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S39A1_HUMAN
ID   S39A1_HUMAN             Reviewed;         324 AA.
AC   Q9NY26; B4DDY7; Q5T4K1; Q8N2H7; Q9BTV0; Q9UBI7; Q9Y2Z7; Q9Y380;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Zinc transporter ZIP1;
DE   AltName: Full=Solute carrier family 39 member 1;
DE   AltName: Full=Zinc-iron-regulated transporter-like;
DE   AltName: Full=Zrt- and Irt-like protein 1;
DE            Short=ZIP-1;
DE            Short=hZIP1;
GN   Name=SLC39A1; Synonyms=IRT1, ZIP1, ZIRTL; ORFNames=CGI-08, CGI-71;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10610721; DOI=10.1006/geno.1999.5993;
RA   Lioumi M., Ferguson C.A., Sharpe P.T., Freeman T., Marenholz I.,
RA   Mischke D., Heizmann C., Ragoussis J.;
RT   "Isolation and characterization of human and mouse ZIRTL, a member of the
RT   IRT1 family of transporters, mapping within the epidermal differentiation
RT   complex.";
RL   Genomics 62:272-280(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX   PubMed=11696349; DOI=10.1016/s0014-5793(01)02950-7;
RA   Milon B., Dhermy D., Pountney D., Bourgeois M., Beaumont C.;
RT   "Differential subcellular localization of hZip1 in adherent and non-
RT   adherent cells.";
RL   FEBS Lett. 507:241-246(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Thyroid, and Urinary bladder;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney, Lung, Muscle, and Placenta;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   CHARACTERIZATION.
RX   PubMed=11301334; DOI=10.1074/jbc.m101772200;
RA   Gaither L.A., Eide D.J.;
RT   "The human ZIP1 transporter mediates zinc uptake in human K562
RT   erythroleukemia cells.";
RL   J. Biol. Chem. 276:22258-22264(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=12888280; DOI=10.1016/s0162-0134(03)00249-6;
RA   Franklin R.B., Ma J., Zou J., Guan Z., Kukoyi B.I., Feng P., Costello L.C.;
RT   "Human ZIP1 is a major zinc uptake transporter for the accumulation of zinc
RT   in prostate cells.";
RL   J. Inorg. Biochem. 96:435-442(2003).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Mediates zinc uptake. May function as a major endogenous zinc
CC       uptake transporter in many cells of the body. Responsible for the rapid
CC       uptake and accumulation of physiologically effective zinc in prostate
CC       cells. {ECO:0000269|PubMed:12888280}.
CC   -!- INTERACTION:
CC       Q9NY26; P21964: COMT; NbExp=3; IntAct=EBI-726491, EBI-372265;
CC       Q9NY26; Q07325: CXCL9; NbExp=3; IntAct=EBI-726491, EBI-3911467;
CC       Q9NY26; P49447: CYB561; NbExp=3; IntAct=EBI-726491, EBI-8646596;
CC       Q9NY26; Q96CV9: OPTN; NbExp=3; IntAct=EBI-726491, EBI-748974;
CC       Q9NY26; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-726491, EBI-2852148;
CC       Q9NY26; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-726491, EBI-11988865;
CC       Q9NY26; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-726491, EBI-751210;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11696349};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:11696349}. Endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:11696349}; Multi-pass membrane
CC       protein {ECO:0000269|PubMed:11696349}. Note=Shows a vesicular
CC       localization corresponding partially to the endoplasmic reticulum in
CC       several epithelial cell lines.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NY26-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NY26-2; Sequence=VSP_056522;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in most adult and fetal
CC       tissues including the epidermis. {ECO:0000269|PubMed:10610721}.
CC   -!- MISCELLANEOUS: Inhibited by Ni(2+) ions. Fe(2+) ions do not inhibit
CC       zinc uptake.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD27717.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SLC39A1ID46571ch1q21.html";
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DR   EMBL; AJ243649; CAB59979.1; -; mRNA.
DR   EMBL; AJ243650; CAB59980.1; -; Genomic_DNA.
DR   EMBL; AJ271671; CAB82784.1; -; mRNA.
DR   EMBL; AF132942; AAD27717.1; ALT_FRAME; mRNA.
DR   EMBL; AF151829; AAD34066.1; -; mRNA.
DR   EMBL; AK075257; BAC11502.1; -; mRNA.
DR   EMBL; AK074943; BAG52035.1; -; mRNA.
DR   EMBL; AK293389; BAG56898.1; -; mRNA.
DR   EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53259.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53261.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53264.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53265.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53267.1; -; Genomic_DNA.
DR   EMBL; BC002563; AAH02563.1; -; mRNA.
DR   EMBL; BC003152; AAH03152.1; -; mRNA.
DR   EMBL; BC007886; AAH07886.1; -; mRNA.
DR   EMBL; BC014303; AAH14303.1; -; mRNA.
DR   CCDS; CCDS1055.1; -. [Q9NY26-1]
DR   RefSeq; NP_001258886.1; NM_001271957.1. [Q9NY26-1]
DR   RefSeq; NP_001258887.1; NM_001271958.1. [Q9NY26-1]
DR   RefSeq; NP_001258888.1; NM_001271959.1. [Q9NY26-1]
DR   RefSeq; NP_001258889.1; NM_001271960.1. [Q9NY26-1]
DR   RefSeq; NP_001258890.1; NM_001271961.1.
DR   RefSeq; NP_055252.2; NM_014437.4. [Q9NY26-1]
DR   AlphaFoldDB; Q9NY26; -.
DR   SMR; Q9NY26; -.
DR   BioGRID; 118050; 47.
DR   IntAct; Q9NY26; 28.
DR   MINT; Q9NY26; -.
DR   STRING; 9606.ENSP00000357612; -.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   TCDB; 2.A.5.3.2; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR   PhosphoSitePlus; Q9NY26; -.
DR   SwissPalm; Q9NY26; -.
DR   BioMuta; SLC39A1; -.
DR   DMDM; 37090460; -.
DR   EPD; Q9NY26; -.
DR   jPOST; Q9NY26; -.
DR   MassIVE; Q9NY26; -.
DR   MaxQB; Q9NY26; -.
DR   PaxDb; Q9NY26; -.
DR   PeptideAtlas; Q9NY26; -.
DR   PRIDE; Q9NY26; -.
DR   ProteomicsDB; 3906; -.
DR   ProteomicsDB; 83153; -. [Q9NY26-1]
DR   Antibodypedia; 20389; 109 antibodies from 27 providers.
DR   DNASU; 27173; -.
DR   Ensembl; ENST00000310483.10; ENSP00000309710.6; ENSG00000143570.19. [Q9NY26-1]
DR   Ensembl; ENST00000356205.9; ENSP00000348535.4; ENSG00000143570.19. [Q9NY26-1]
DR   Ensembl; ENST00000368621.5; ENSP00000357610.1; ENSG00000143570.19. [Q9NY26-1]
DR   Ensembl; ENST00000368623.7; ENSP00000357612.3; ENSG00000143570.19. [Q9NY26-1]
DR   Ensembl; ENST00000617697.4; ENSP00000479421.1; ENSG00000143570.19. [Q9NY26-1]
DR   Ensembl; ENST00000621013.4; ENSP00000484182.1; ENSG00000143570.19. [Q9NY26-1]
DR   GeneID; 27173; -.
DR   KEGG; hsa:27173; -.
DR   MANE-Select; ENST00000356205.9; ENSP00000348535.4; NM_001271958.2; NP_001258887.1.
DR   UCSC; uc001fdi.5; human. [Q9NY26-1]
DR   CTD; 27173; -.
DR   DisGeNET; 27173; -.
DR   GeneCards; SLC39A1; -.
DR   HGNC; HGNC:12876; SLC39A1.
DR   HPA; ENSG00000143570; Low tissue specificity.
DR   MIM; 604740; gene.
DR   neXtProt; NX_Q9NY26; -.
DR   OpenTargets; ENSG00000143570; -.
DR   PharmGKB; PA37465; -.
DR   VEuPathDB; HostDB:ENSG00000143570; -.
DR   eggNOG; KOG1558; Eukaryota.
DR   GeneTree; ENSGT00940000157062; -.
DR   InParanoid; Q9NY26; -.
DR   OMA; HSSLHTD; -.
DR   OrthoDB; 981397at2759; -.
DR   PhylomeDB; Q9NY26; -.
DR   TreeFam; TF317098; -.
DR   PathwayCommons; Q9NY26; -.
DR   Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family.
DR   SignaLink; Q9NY26; -.
DR   BioGRID-ORCS; 27173; 24 hits in 1085 CRISPR screens.
DR   ChiTaRS; SLC39A1; human.
DR   GeneWiki; SLC39A1; -.
DR   GenomeRNAi; 27173; -.
DR   Pharos; Q9NY26; Tbio.
DR   PRO; PR:Q9NY26; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9NY26; protein.
DR   Bgee; ENSG00000143570; Expressed in placenta and 95 other tissues.
DR   ExpressionAtlas; Q9NY26; baseline and differential.
DR   Genevisible; Q9NY26; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0022890; F:inorganic cation transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006812; P:cation transport; TAS:ProtInc.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0060173; P:limb development; IEA:Ensembl.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; IMP:UniProtKB.
DR   InterPro; IPR003689; ZIP.
DR   Pfam; PF02535; Zip; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Endoplasmic reticulum; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport; Zinc; Zinc transport.
FT   CHAIN           1..324
FT                   /note="Zinc transporter ZIP1"
FT                   /id="PRO_0000068763"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..104
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..272
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..303
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..106
FT                   /note="MGPWGEPELLVWRPEAVASEPPVPVGLEVKLGALVLLLVLTLLCSLVPICVL
FT                   RRPGANHEGSASRQKALSLVSCFAGGVFLATCLLDLLPDYLAAIDEALAALHVT -> M
FT                   KAQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056522"
FT   CONFLICT        10..18
FT                   /note="LVWRPEAVA -> HGVAPRGGT (in Ref. 3; AAD34066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="A -> S (in Ref. 8; AAH03152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47..50
FT                   /note="VPIC -> GSIG (in Ref. 1; CAB59979/CAB59980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="P -> T (in Ref. 1; CAB59979/CAB59980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="F -> V (in Ref. 3; AAD27717/AAD34066)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="R -> G (in Ref. 4; BAC11502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   324 AA;  34250 MW;  884C168AA8E8C0DF CRC64;
     MGPWGEPELL VWRPEAVASE PPVPVGLEVK LGALVLLLVL TLLCSLVPIC VLRRPGANHE
     GSASRQKALS LVSCFAGGVF LATCLLDLLP DYLAAIDEAL AALHVTLQFP LQEFILAMGF
     FLVLVMEQIT LAYKEQSGPS PLEETRALLG TVNGGPQHWH DGPGVPQASG APATPSALRA
     CVLVFSLALH SVFEGLAVGL QRDRARAMEL CLALLLHKGI LAVSLSLRLL QSHLRAQVVA
     GCGILFSCMT PLGIGLGAAL AESAGPLHQL AQSVLEGMAA GTFLYITFLE ILPQELASSE
     QRILKVILLL AGFALLTGLL FIQI
 
 
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