STEA2_HUMAN
ID STEA2_HUMAN Reviewed; 490 AA.
AC Q8NFT2; A4D1F1; G5E9C6; Q6UXN6; Q6YPB1; Q8IUE7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Metalloreductase STEAP2;
DE EC=1.16.1.-;
DE AltName: Full=Prostate cancer-associated protein 1;
DE AltName: Full=Protein up-regulated in metastatic prostate cancer;
DE Short=PUMPCn;
DE AltName: Full=Six-transmembrane epithelial antigen of prostate 2;
DE AltName: Full=SixTransMembrane protein of prostate 1;
GN Name=STEAP2; Synonyms=PCANAP1, STAMP1; ORFNames=UNQ6507/PRO23203;
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 [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP VARIANTS CYS-17 AND ILE-475.
RC TISSUE=Prostate;
RX PubMed=12095985; DOI=10.1074/jbc.m202414200;
RA Korkmaz K.S., Elbi C.C., Korkmaz C.G., Loda M., Hager G.L., Saatcioglu F.;
RT "Molecular cloning and characterization of STAMP1, a highly prostate
RT specific six-trans-membrane protein that is overexpressed in prostate
RT cancer.";
RL J. Biol. Chem. 277:36689-36696(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND VARIANTS CYS-17; GLN-456 AND ILE-475.
RC TISSUE=Prostate;
RX PubMed=12429817; DOI=10.1097/01.lab.0000038554.26102.c6;
RA Porkka K.P., Helenius M.A., Visakorpi T.;
RT "Cloning and characterization of a novel six-transmembrane protein STEAP2,
RT expressed in normal and malignant prostate.";
RL Lab. Invest. 82:1573-1582(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT CYS-17.
RA Zhang Z., Eberhard D.A., Polakis P., Grimaldi C., Frantz G.D., Hillan K.J.,
RA Wood W.I.;
RT "Bioinformatics identification and clinical validation of tumor antigens by
RT analysis of EST and tissue microarray data.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT CYS-17.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX 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., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., 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., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-475.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-475.
RA Mural R.J., Istrail S., Sutton G.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 TISSUE SPECIFICITY.
RX PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
RA Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
RT "The Steap proteins are metalloreductases.";
RL Blood 108:1388-1394(2006).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-17, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Metalloreductase that has the ability to reduce both Fe(3+)
CC to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q687X5};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:12429817}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12429817}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NFT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFT2-2; Sequence=VSP_030999;
CC Name=3;
CC IsoId=Q8NFT2-3; Sequence=VSP_045590;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in prostate and at
CC significantly lower levels in heart, brain, kidney, pancreas, and
CC ovary. {ECO:0000269|PubMed:12095985, ECO:0000269|PubMed:12429817,
CC ECO:0000269|PubMed:16609065}.
CC -!- SIMILARITY: Belongs to the STEAP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/STEAP2ID42435ch7q21.html";
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DR EMBL; AY008444; AAG32148.1; -; mRNA.
DR EMBL; AY008445; AAG32149.1; -; mRNA.
DR EMBL; AF455138; AAN04080.1; -; mRNA.
DR EMBL; AF526382; AAQ08976.1; -; mRNA.
DR EMBL; AY358267; AAQ88634.1; -; mRNA.
DR EMBL; AC002064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236949; EAL24165.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76890.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76894.1; -; Genomic_DNA.
DR CCDS; CCDS43612.1; -. [Q8NFT2-2]
DR CCDS; CCDS5615.1; -. [Q8NFT2-1]
DR CCDS; CCDS59064.1; -. [Q8NFT2-3]
DR RefSeq; NP_001035755.1; NM_001040665.1. [Q8NFT2-1]
DR RefSeq; NP_001035756.1; NM_001040666.1. [Q8NFT2-2]
DR RefSeq; NP_001231873.1; NM_001244944.1. [Q8NFT2-1]
DR RefSeq; NP_001231875.1; NM_001244946.1. [Q8NFT2-3]
DR RefSeq; NP_694544.2; NM_152999.3. [Q8NFT2-1]
DR RefSeq; XP_006715984.1; XM_006715921.3. [Q8NFT2-1]
DR RefSeq; XP_016867442.1; XM_017011953.1. [Q8NFT2-1]
DR RefSeq; XP_016867443.1; XM_017011954.1. [Q8NFT2-1]
DR AlphaFoldDB; Q8NFT2; -.
DR SMR; Q8NFT2; -.
DR BioGRID; 129285; 17.
DR CORUM; Q8NFT2; -.
DR IntAct; Q8NFT2; 7.
DR STRING; 9606.ENSP00000378119; -.
DR TCDB; 5.B.6.1.2; the transmembrane epithelial antigen protein-3 ferric reductase (steap) family.
DR iPTMnet; Q8NFT2; -.
DR PhosphoSitePlus; Q8NFT2; -.
DR SwissPalm; Q8NFT2; -.
DR BioMuta; STEAP2; -.
DR DMDM; 296452950; -.
DR EPD; Q8NFT2; -.
DR jPOST; Q8NFT2; -.
DR MassIVE; Q8NFT2; -.
DR MaxQB; Q8NFT2; -.
DR PaxDb; Q8NFT2; -.
DR PeptideAtlas; Q8NFT2; -.
DR PRIDE; Q8NFT2; -.
DR ProteomicsDB; 33900; -.
DR ProteomicsDB; 73348; -. [Q8NFT2-1]
DR ProteomicsDB; 73349; -. [Q8NFT2-2]
DR Antibodypedia; 29828; 214 antibodies from 30 providers.
DR DNASU; 261729; -.
DR Ensembl; ENST00000287908.7; ENSP00000287908.3; ENSG00000157214.14. [Q8NFT2-1]
DR Ensembl; ENST00000394621.7; ENSP00000378119.2; ENSG00000157214.14. [Q8NFT2-1]
DR Ensembl; ENST00000394622.6; ENSP00000378120.2; ENSG00000157214.14. [Q8NFT2-1]
DR Ensembl; ENST00000394626.5; ENSP00000378123.1; ENSG00000157214.14. [Q8NFT2-2]
DR Ensembl; ENST00000394629.2; ENSP00000378125.2; ENSG00000157214.14. [Q8NFT2-2]
DR Ensembl; ENST00000394632.5; ENSP00000378128.1; ENSG00000157214.14. [Q8NFT2-3]
DR GeneID; 261729; -.
DR KEGG; hsa:261729; -.
DR MANE-Select; ENST00000394621.7; ENSP00000378119.2; NM_001244944.2; NP_001231873.1.
DR UCSC; uc003ujz.4; human. [Q8NFT2-1]
DR CTD; 261729; -.
DR DisGeNET; 261729; -.
DR GeneCards; STEAP2; -.
DR HGNC; HGNC:17885; STEAP2.
DR HPA; ENSG00000157214; Tissue enriched (prostate).
DR MIM; 605094; gene.
DR neXtProt; NX_Q8NFT2; -.
DR OpenTargets; ENSG00000157214; -.
DR PharmGKB; PA38473; -.
DR VEuPathDB; HostDB:ENSG00000157214; -.
DR eggNOG; ENOG502QVSJ; Eukaryota.
DR GeneTree; ENSGT00390000008042; -.
DR InParanoid; Q8NFT2; -.
DR OMA; AKTNIIF; -.
DR PhylomeDB; Q8NFT2; -.
DR TreeFam; TF332031; -.
DR PathwayCommons; Q8NFT2; -.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR SignaLink; Q8NFT2; -.
DR BioGRID-ORCS; 261729; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; STEAP2; human.
DR GeneWiki; STEAP2; -.
DR GenomeRNAi; 261729; -.
DR Pharos; Q8NFT2; Tbio.
DR PRO; PR:Q8NFT2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8NFT2; protein.
DR Bgee; ENSG00000157214; Expressed in pericardium and 178 other tissues.
DR ExpressionAtlas; Q8NFT2; baseline and differential.
DR Genevisible; Q8NFT2; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB.
DR GO; GO:0008823; F:cupric reductase activity; IBA:GO_Central.
DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015677; P:copper ion import; IBA:GO_Central.
DR GO; GO:0098705; P:copper ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IDA:UniProtKB.
DR GO; GO:0098711; P:iron ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0045055; P:regulated exocytosis; IDA:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Copper; Electron transport; Endosome;
KW FAD; Flavoprotein; Heme; Ion transport; Iron; Iron transport; Membrane;
KW Metal-binding; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..490
FT /note="Metalloreductase STEAP2"
FT /id="PRO_0000191697"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 259..407
FT /note="Ferric oxidoreductase"
FT BINDING 38..41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 60..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 93..100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 118
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q658P3"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 316
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 395
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT BINDING 409
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q687X5"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWB6"
FT VAR_SEQ 396..490
FT /note="STLGYVALLISTFHVLIYGWKRAFEEEYYRFYTPPNFVLALVLPSIVILGKI
FT ILFLPCISRKLKRIKKGWEKSQFLEEGMGGTIPHVSPERVTVM -> IFCSFADTQTEL
FT ELEFVFLLTLLL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12095985"
FT /id="VSP_045590"
FT VAR_SEQ 445..490
FT /note="GKIILFLPCISRKLKRIKKGWEKSQFLEEGMGGTIPHVSPERVTVM -> DL
FT LQLCRYPD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309, ECO:0000303|Ref.3"
FT /id="VSP_030999"
FT VARIANT 17
FT /note="F -> C (in dbSNP:rs194520)"
FT /evidence="ECO:0000269|PubMed:12095985,
FT ECO:0000269|PubMed:12429817, ECO:0000269|PubMed:12975309,
FT ECO:0000269|Ref.3, ECO:0007744|PubMed:18669648"
FT /id="VAR_060387"
FT VARIANT 40
FT /note="D -> Y (in dbSNP:rs17863046)"
FT /id="VAR_060388"
FT VARIANT 214
FT /note="G -> E (in dbSNP:rs13228098)"
FT /id="VAR_057727"
FT VARIANT 456
FT /note="R -> Q (in dbSNP:rs194524)"
FT /evidence="ECO:0000269|PubMed:12429817"
FT /id="VAR_057728"
FT VARIANT 475
FT /note="M -> I (in dbSNP:rs194525)"
FT /evidence="ECO:0000269|PubMed:12095985,
FT ECO:0000269|PubMed:12429817, ECO:0000269|PubMed:12690205,
FT ECO:0000269|Ref.7"
FT /id="VAR_060389"
FT CONFLICT 17
FT /note="F -> V (in Ref. 2; AAN04080)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> F (in Ref. 1; AAG32148/AAG32149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56056 MW; DB12E252DE3F4CAF CRC64;
MESISMMGSP KSLSETFLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS
RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM
RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE
LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA
RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ
CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY
ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE
EEYYRFYTPP NFVLALVLPS IVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGMGGTIP
HVSPERVTVM
