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";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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