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AQP1_HUMAN.sp
ID AQP1_HUMAN Reviewed; 269 AA.
AC P29972; B5BU39; Q8TBI5; Q8TDC1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 18-MAY-2010, entry version 122.
DE RecName: Full=Aquaporin-1;
DE Short=AQP-1;
DE AltName: Full=Aquaporin-CHIP;
DE AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
DE AltName: Full=Urine water channel;
GN Name=AQP1; Synonyms=CHIP28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX MEDLINE=92107900; PubMed=1722319; DOI=10.1073/pnas.88.24.11110;
RA Preston G.M., Agre P.;
RT "Isolation of the cDNA for erythrocyte integral membrane protein of 28
RT kilodaltons: member of an ancient channel family.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=93340184; PubMed=8340403;
RA Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.;
RT "The human aquaporin-CHIP gene. Structure, organization, and
RT chromosomal localization.";
RL J. Biol. Chem. 268:15772-15778(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retinal pigment epithelium;
RX MEDLINE=96326579; PubMed=8703970; DOI=10.1016/0005-2736(96)00076-4;
RA Ruiz A.C., Bok D.;
RT "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in
RT human retinal pigment epithelium.";
RL Biochim. Biophys. Acta 1282:174-178(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RX MEDLINE=94290349; PubMed=7517253;
RA Li X., Yu H., Koide S.S.;
RT "The water channel gene in human uterus.";
RL Biochem. Mol. Biol. Int. 32:371-377(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269.
RC TISSUE=Articular cartilage;
RA Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.;
RT "Human chondrocytes in situ express aquaporin water channels: changes
RT in AQP1 abundance in pathologies of articular cartilage.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP PROTEIN SEQUENCE OF 2-36.
RX PubMed=2007592;
RA Smith B.L., Agre P.;
RT "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit
RT oligomer similar to channel proteins.";
RL J. Biol. Chem. 266:6407-6415(1991).
RN [12]
RP FUNCTION.
RX MEDLINE=92229472; PubMed=1373524; DOI=10.1126/science.256.5055.385;
RA Preston G.M., Carroll T.P., Guggino W.B., Agre P.;
RT "Appearance of water channels in Xenopus oocytes expressing red cell
RT CHIP28 protein.";
RL Science 256:385-387(1992).
RN [13]
RP TARGET OF MERCURY INHIBITION.
RX MEDLINE=93106996; PubMed=7677994;
RA Preston G.M., Jung J.S., Guggino W.B., Agre P.;
RT "The mercury-sensitive residue at cysteine 189 in the CHIP28 water
RT channel.";
RL J. Biol. Chem. 268:17-20(1993).
RN [14]
RP TOPOLOGY.
RX MEDLINE=94124503; PubMed=7507481;
RA Preston G.M., Jung J.S., Guggino W.B., Agre P.;
RT "Membrane topology of aquaporin CHIP. Analysis of functional epitope-
RT scanning mutants by vectorial proteolysis.";
RL J. Biol. Chem. 269:1668-1673(1994).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASS
RP SPECTROMETRY.
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
RX MEDLINE=94313979; PubMed=7518771;
RA Walz T., Smith B.L., Agre P., Engel A.;
RT "The three-dimensional structure of human erythrocyte aquaporin
RT CHIP.";
RL EMBO J. 13:2985-2993(1994).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
RX MEDLINE=97320502; PubMed=9177353; DOI=10.1038/42512;
RA Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y.,
RA Smith B.L., Agre P., Engel A.;
RT "The three-dimensional structure of aquaporin-1.";
RL Nature 387:624-627(1997).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
RX MEDLINE=20487015; PubMed=11034202; DOI=10.1038/35036519;
RA Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B.,
RA Engel A., Fujiyoshi Y.;
RT "Structural determinants of water permeation through aquaporin-1.";
RL Nature 407:599-605(2000).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
RX MEDLINE=21423577; PubMed=11532455; DOI=10.1016/S0014-5793(01)02743-0;
RA de Groot B.L., Engel A., Grubmueller H.;
RT "A refined structure of human aquaporin-1.";
RL FEBS Lett. 504:206-211(2001).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
RX PubMed=11171962; DOI=10.1073/pnas.041489198;
RA Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.;
RT "Visualization of a water-selective pore by electron crystallography
RT in vitreous ice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001).
RN [21]
RP VARIANT BLOOD GROUP COLTON VAL-45.
RX MEDLINE=94365170; PubMed=7521882; DOI=10.1172/JCI117418;
RA Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.;
RT "Human red cell aquaporin CHIP. I. Molecular characterization of ABH
RT and Colton blood group antigens.";
RL J. Clin. Invest. 94:1043-1049(1994).
RN [22]
RP VARIANT LEU-38.
RX MEDLINE=94360246; PubMed=7521540; DOI=10.1126/science.7521540;
RA Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.;
RT "Mutations in aquaporin-1 in phenotypically normal humans without
RT functional CHIP water channels.";
RL Science 265:1585-1587(1994).
CC -!- FUNCTION: Forms a water-specific channel that provides the plasma
CC membranes of red cells and kidney proximal tubules with high
CC permeability to water, thereby permitting water to move in the
CC direction of an osmotic gradient.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC Q99750:MDFI; NbExp=3; IntAct=EBI-745213, EBI-724076;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in a number of tissues including
CC erythrocytes, renal tubules, retinal pigment epithelium, heart,
CC lung, skeletal muscle, kidney and pancreas. Weakly expressed in
CC brain, placenta and liver.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing
CC three membrane-spanning domains and a pore-forming loop with the
CC signature motif Asn-Pro-Ala (NPA).
CC -!- POLYMORPHISM: AQP1 is responsible for the Colton blood group
CC system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46),
CC approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val-
CC 46). Co(A-B-) which is very rare, is due to a complete absence of
CC AQP1.
CC -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC concentrations of mercury.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC mutation database;
CC URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=colton";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/aqp1/";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue
CC 36 of July 2003;
CC URL="http://www.expasy.org/spotlight/back_issues/sptlt036.shtml";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M77829; AAA58425.1; -; mRNA.
DR EMBL; U41517; AAC50648.1; -; mRNA.
DR EMBL; U41518; AAC50649.1; -; mRNA.
DR EMBL; S73482; AAB31193.1; -; mRNA.
DR EMBL; AC004691; AAC16481.1; -; Genomic_DNA.
DR EMBL; AC005155; AAC23788.1; -; Genomic_DNA.
DR EMBL; AY953319; AAX24129.1; -; Genomic_DNA.
DR EMBL; AB451275; BAG70089.1; -; mRNA.
DR EMBL; AB451402; BAG70216.1; -; mRNA.
DR EMBL; CH471073; EAW93971.1; -; Genomic_DNA.
DR EMBL; BC022486; AAH22486.1; -; mRNA.
DR EMBL; AF480415; AAL87136.1; -; Genomic_DNA.
DR IPI; IPI00024689; -.
DR PIR; A41616; A41616.
DR PIR; I52366; I52366.
DR RefSeq; NP_932766.1; -.
DR UniGene; Hs.76152; -.
DR PDB; 1FQY; X-ray; 3.80 A; A=1-269.
DR PDB; 1H6I; X-ray; 3.54 A; A=1-269.
DR PDB; 1IH5; X-ray; 3.70 A; A=1-269.
DR PDBsum; 1FQY; -.
DR PDBsum; 1H6I; -.
DR PDBsum; 1IH5; -.
DR SMR; P29972; 8-233.
DR DIP; DIP-29607N; -.
DR IntAct; P29972; 7.
DR MINT; MINT-1439356; -.
DR STRING; P29972; -.
DR TCDB; 1.A.8.8.1; major intrinsic protein (MIP) family.
DR PhosphoSite; P29972; -.
DR PRIDE; P29972; -.
DR Ensembl; ENST00000311813; ENSP00000311165; ENSG00000240583; Homo sapiens.
DR GeneID; 358; -.
DR KEGG; hsa:358; -.
DR UCSC; uc003tbv.1; human.
DR CTD; 358; -.
DR GeneCards; GC07P030917; -.
DR HGNC; HGNC:633; AQP1.
DR HPA; CAB001707; -.
DR HPA; HPA019206; -.
DR MIM; 107776; gene.
DR MIM; 110450; phenotype.
DR PharmGKB; PA24918; -.
DR eggNOG; prNOG13886; -.
DR HOVERGEN; HBG000312; -.
DR InParanoid; P29972; -.
DR OMA; TGCSINP; -.
DR PhylomeDB; P29972; -.
DR DrugBank; DB00819; Acetazolamide.
DR NextBio; 1497; -.
DR ArrayExpress; P29972; -.
DR Bgee; P29972; -.
DR CleanEx; HS_AQP1; -.
DR Genevestigator; P29972; -.
DR GermOnline; ENSG00000106125; Homo sapiens.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0051739; F:ammonia transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0035379; F:carbon dioxide transmembrane transporter ac...; IDA:UniProtKB.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005223; F:intracellular cGMP activated cation channel...; IDA:UniProtKB.
DR GO; GO:0030184; F:nitric oxide transmembrane transporter acti...; IDA:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IMP:UniProtKB.
DR GO; GO:0015079; F:potassium ion transmembrane transporter act...; ISS:UniProtKB.
DR GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0015696; P:ammonium transport; IDA:UniProtKB.
DR GO; GO:0035378; P:carbon dioxide transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:UniProtKB.
DR GO; GO:0071474; P:cellular hyperosmotic response; IMP:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
DR GO; GO:0071288; P:cellular response to mercury ion; IDA:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0033326; P:cerebrospinal fluid secretion; IEP:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030950; P:establishment or maintenance of actin cytos...; IMP:UniProtKB.
DR GO; GO:0015793; P:glycerol transport; IDA:UniProtKB.
DR GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptosis; IDA:UniProtKB.
DR GO; GO:0030185; P:nitric oxide transport; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
DR GO; GO:0030157; P:pancreatic juice secretion; IEP:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast prolifera...; IDA:UniProtKB.
DR GO; GO:0046878; P:positive regulation of saliva secretion; IMP:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0003097; P:renal water transport; IDA:UniProtKB.
DR GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR GO; GO:0035377; P:transepithelial water transport; IDA:UniProtKB.
DR InterPro; IPR012269; Aquaporin.
DR InterPro; IPR000425; MIP.
DR Gene3D; G3DSA:1.20.1080.10; MIP; 1.
DR PANTHER; PTHR19139; MIP; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; MIP; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood group antigen; Complete proteome;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Polymorphism; Repeat; Transmembrane; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 269 Aquaporin-1.
FT /FTId=PRO_0000063920.
FT TOPO_DOM 2 7 Cytoplasmic.
FT TRANSMEM 8 36 Helix 1.
FT TOPO_DOM 37 48 Extracellular.
FT TRANSMEM 49 66 Helix 2.
FT TOPO_DOM 67 70 Cytoplasmic.
FT TOPO_DOM 71 76 In membrane.
FT TRANSMEM 77 84 Helix B.
FT TOPO_DOM 85 94 Cytoplasmic.
FT TRANSMEM 95 115 Helix 3.
FT TOPO_DOM 116 136 Extracellular.
FT TRANSMEM 137 155 Helix 4.
FT TOPO_DOM 156 166 Cytoplasmic.
FT TRANSMEM 167 183 Helix 5.
FT TOPO_DOM 184 186 Extracellular.
FT TOPO_DOM 187 192 In membrane.
FT TRANSMEM 193 200 Helix E.
FT TOPO_DOM 201 207 Extracellular.
FT TRANSMEM 208 228 Helix 6.
FT TOPO_DOM 229 269 Cytoplasmic.
FT MOTIF 76 78 NPA 1.
FT MOTIF 192 194 NPA 2.
FT COMPBIAS 159 162 Poly-Arg.
FT SITE 56 56 Substrate discrimination.
FT SITE 180 180 Substrate discrimination.
FT SITE 189 189 Hg(2+)-sensitive residue.
FT SITE 195 195 Substrate discrimination.
FT MOD_RES 246 246 Phosphothreonine (By similarity).
FT MOD_RES 247 247 Phosphoserine (By similarity).
FT MOD_RES 262 262 Phosphoserine.
FT CARBOHYD 42 42 N-linked (GlcNAc...).
FT CARBOHYD 205 205 N-linked (GlcNAc...) (Potential).
FT VARIANT 38 38 P -> L (in Co(A-B-) antigen; non
FT functional AQP1; red cells show low
FT osmotic water permeability).
FT /FTId=VAR_013279.
FT VARIANT 45 45 A -> V (in Co(A-B+) antigen;
FT dbSNP:rs28362692).
FT /FTId=VAR_004400.
FT VARIANT 165 165 G -> D (in dbSNP:rs28362731).
FT /FTId=VAR_022318.
FT CONFLICT 45 45 A -> T (in Ref. 9; AAH22486).
FT HELIX 8 35
FT STRAND 37 42
FT HELIX 48 65
FT STRAND 68 71
FT HELIX 76 83
FT HELIX 94 114
FT TURN 119 122
FT STRAND 132 135
FT HELIX 136 154
FT HELIX 166 182
FT TURN 183 185
FT HELIX 192 199
FT HELIX 207 227
SQ SEQUENCE 269 AA; 28526 MW; BA204D82FB26352E CRC64;
MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI
ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT
GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH
LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD
RVKVWTSGQV EEYDLDADDI NSRVEMKPK
//
Raw
Rakmakallan_clean.pl
#!/usr/bin/perl -w
use Modern::Perl;
open (my $EPIC,"<", $ARGV[0]);
my ($ID, $AC, $SEQ);
while (<$EPIC>) {
if (m/^ID\s{3}(\S*)\s/gi) {$ID=$1;}
if (m/^AC\s{3}(\S*)\;/gi) {
$AC=$1;
print ">$ID $AC\n";
}
if (m/^\s{5}(.+)/gi) {
$SEQ .= $1;
$SEQ =~ s/\s//g;
}
}
print "$SEQ\n";
my @res=split("",$SEQ);
my $helcount=0;
my $lala=length($SEQ);
my @observed;
for (my $obcount=0;$obcount<=$lala-1;$obcount++)
{$observed[$obcount]='nonhydro';}
#print "@observed";
open (EPIC,"$ARGV[0]");
while (<EPIC>)
{if ($_=~m/^FT\s{3}TRANSMEM\s*(\d*)\s*(\d*)/gi)
{print "\n";
$helcount++;
print "TM$helcount $1 $2 ";
for (my $trans=$1;$trans<=$2;$trans++)
{print $res[$trans];
$observed[$trans]='hydro';}}}
#print "@observed";
print "\n";
my %KD = ('A'=>'1.8',
'R'=>'-4.5',
'N'=>'-3.5',
'D'=>'-3.5',
'C'=>'2.5',
'Q'=>'-3.5',
'E'=>'-3.5',
'G'=>'-0.4',
'H'=>'-3.2',
'I'=>'4.5',
'L'=>'3.8',
'K'=>'-3.9',
'M'=>'1.9',
'F'=>'2.8',
'P'=>'-1.6',
'S'=>'-0.8',
'T'=>'-0.7',
'W'=>'-0.9',
'Y'=>'-1.3',
'V'=>'4.2');
my @predicted=("nonhydro","nonhydro","nonhydro","nonhydro","nonhydro","nonhydro","nonhydro","nonhydro","nonhydro");
my $arith=0;
for (my $i=10;$i<=$lala-9;$i++) {
for (my $add=-10;$add<=9;$add++) {
my $mediator=$res[$i+$add];
die "$mediator does not exist in \%KD" if !exists $KD{$mediator};
$arith=$arith+$KD{$mediator};
}
my $hydrocount=$arith/20;
print "$hydrocount\n";
if ($hydrocount>=0) {push (@predicted,'hydro');}
if ($hydrocount<0) {push (@predicted,'nonhydro');}
$arith=0;
}
my ($tp, $tn, $fp, $fn);
for (my $compcount=0;$compcount<=$#observed;$compcount++) {
if ($predicted[$compcount] eq $observed[$compcount]) {
if ($observed[$compcount] eq "hydro") {$tp++;}
if ($observed[$compcount] eq "nonhydro") {$tn++;}
} else {
if ($observed[$compcount] eq "hydro") {$fn++;}
if ($observed[$compcount] eq "nonhydro") {$fp++;}
}
}
my $Q=($tp+$tn)/($tp+$tn+$fp+$fn);
print "Q=$Q\n";
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