GALT3_HUMAN
ID GALT3_HUMAN Reviewed; 633 AA.
AC Q14435; Q53TG9; Q7Z476;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 3;
DE Short=GalNAc-T3;
DE Short=pp-GaNTase 3;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 3;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3;
GN Name=GALNT3;
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] (ISOFORM 1), ENZYME ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Salivary gland;
RX PubMed=8663203; DOI=10.1074/jbc.271.29.17006;
RA Bennett E.P., Hassan H., Clausen H.;
RT "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-
RT galactosamine polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3.";
RL J. Biol. Chem. 271:17006-17012(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 [5]
RP FUNCTION.
RX PubMed=9295285; DOI=10.1074/jbc.272.38.23503;
RA Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P.,
RA Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J.,
RA Taylor-Papadimitriou J., Clausen H.;
RT "Substrate specificities of three members of the human UDP-N-acetyl-alpha-
RT D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family,
RT GalNAc-T1, -T2, and -T3.";
RL J. Biol. Chem. 272:23503-23514(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9394011; DOI=10.1242/jcs.111.1.45;
RA Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P.,
RA Whitehouse C., Berger E.G., Clausen H., Nilsson T.;
RT "Localization of three human polypeptide GalNAc-transferases in HeLa cells
RT suggests initiation of O-linked glycosylation throughout the Golgi
RT apparatus.";
RL J. Cell Sci. 111:45-60(1998).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12708471; DOI=10.1111/j.1349-7006.2003.tb01348.x;
RA Onitsuka K., Shibao K., Nakayama Y., Minagawa N., Hirata K., Izumi H.,
RA Matsuo K., Nagata N., Kitazato K., Kohno K., Itoh H.;
RT "Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide
RT N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with
RT gastric carcinoma.";
RL Cancer Sci. 94:32-36(2003).
RN [8]
RP INVOLVEMENT IN HFTC1, AND VARIANT HFTC 162-ARG--ASP-633 DEL.
RX PubMed=15133511; DOI=10.1038/ng1358;
RA Topaz O., Shurman D.L., Bergman R., Indelman M., Ratajczak P., Mizrachi M.,
RA Khamaysi Z., Behar D., Petronius D., Friedman V., Zelikovic I., Raimer S.,
RA Metzker A., Richard G., Sprecher E.;
RT "Mutations in GALNT3, encoding a protein involved in O-linked
RT glycosylation, cause familial tumoral calcinosis.";
RL Nat. Genet. 36:579-581(2004).
RN [9]
RP INVOLVEMENT IN HFTC1.
RX PubMed=15599692; DOI=10.1007/s00109-004-0610-8;
RA Frishberg Y., Topaz O., Bergman R., Behar D., Fisher D., Gordon D.,
RA Richard G., Sprecher E.;
RT "Identification of a recurrent mutation in GALNT3 demonstrates that
RT hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are
RT allelic disorders.";
RL J. Mol. Med. 83:33-38(2005).
RN [10]
RP FUNCTION.
RX PubMed=16638743; DOI=10.1074/jbc.m602469200;
RA Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B.,
RA Bennett E.P., Mandel U., Strom T.M., Clausen H.;
RT "Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis.
RT Secretion of fibroblast growth factor 23 requires O-glycosylation.";
RL J. Biol. Chem. 281:18370-18377(2006).
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: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has activity
CC toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably
CC glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central
CC role in phosphate homeostasis. {ECO:0000269|PubMed:16638743,
CC ECO:0000269|PubMed:9295285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:8663203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:8663203};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q14435-2; Q92624: APPBP2; NbExp=3; IntAct=EBI-10232904, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the trans
CC and medial parts of the Golgi stack.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14435-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14435-2; Sequence=VSP_011202, VSP_011203;
CC -!- TISSUE SPECIFICITY: Expressed in organs that contain secretory
CC epithelial glands. Highly expressed in pancreas, skin, kidney and
CC testis. Weakly expressed in prostate, ovary, intestine and colon. Also
CC expressed in placenta and lung and fetal lung and fetal kidney.
CC {ECO:0000269|PubMed:12708471, ECO:0000269|PubMed:8663203}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- DISEASE: Tumoral calcinosis, hyperphosphatemic, familial, 1 (HFTC1)
CC [MIM:211900]: A form of hyperphosphatemic tumoral calcinosis, a rare
CC autosomal recessive metabolic disorder that manifests with
CC hyperphosphatemia and massive calcium deposits in the skin and
CC subcutaneous tissues. Some patients have recurrent, transient, painful
CC swellings of the long bones associated with the radiographic findings
CC of periosteal reaction and cortical hyperostosis and absence of skin
CC involvement. {ECO:0000269|PubMed:15133511,
CC ECO:0000269|PubMed:15599692}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Overexpressed in many differentiated carcinomas,
CC suggesting that it may serve as a marker of tumor differentiation.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_485";
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DR EMBL; X92689; CAA63371.1; -; mRNA.
DR EMBL; AC009495; AAY14678.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11324.1; -; Genomic_DNA.
DR EMBL; BC056246; AAH56246.1; ALT_INIT; mRNA.
DR EMBL; BC113565; AAI13566.1; -; mRNA.
DR EMBL; BC113567; AAI13568.1; -; mRNA.
DR CCDS; CCDS2226.1; -. [Q14435-1]
DR RefSeq; NP_004473.2; NM_004482.3. [Q14435-1]
DR RefSeq; XP_005246506.1; XM_005246449.1. [Q14435-1]
DR RefSeq; XP_011509231.1; XM_011510929.1. [Q14435-1]
DR RefSeq; XP_016859259.1; XM_017003770.1. [Q14435-1]
DR AlphaFoldDB; Q14435; -.
DR SMR; Q14435; -.
DR BioGRID; 108863; 25.
DR IntAct; Q14435; 6.
DR STRING; 9606.ENSP00000376465; -.
DR BindingDB; Q14435; -.
DR ChEMBL; CHEMBL4523291; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyConnect; 1620; 3 N-Linked glycans (1 site).
DR GlyGen; Q14435; 3 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q14435; -.
DR PhosphoSitePlus; Q14435; -.
DR BioMuta; GALNT3; -.
DR DMDM; 209572629; -.
DR EPD; Q14435; -.
DR jPOST; Q14435; -.
DR MassIVE; Q14435; -.
DR MaxQB; Q14435; -.
DR PaxDb; Q14435; -.
DR PeptideAtlas; Q14435; -.
DR PRIDE; Q14435; -.
DR ProteomicsDB; 59988; -. [Q14435-1]
DR ProteomicsDB; 59989; -. [Q14435-2]
DR Antibodypedia; 2358; 171 antibodies from 24 providers.
DR DNASU; 2591; -.
DR Ensembl; ENST00000392701.8; ENSP00000376465.3; ENSG00000115339.14. [Q14435-1]
DR GeneID; 2591; -.
DR KEGG; hsa:2591; -.
DR MANE-Select; ENST00000392701.8; ENSP00000376465.3; NM_004482.4; NP_004473.2.
DR UCSC; uc010fph.2; human. [Q14435-1]
DR CTD; 2591; -.
DR DisGeNET; 2591; -.
DR GeneCards; GALNT3; -.
DR GeneReviews; GALNT3; -.
DR HGNC; HGNC:4125; GALNT3.
DR HPA; ENSG00000115339; Tissue enhanced (stomach).
DR MalaCards; GALNT3; -.
DR MIM; 211900; phenotype.
DR MIM; 601756; gene.
DR neXtProt; NX_Q14435; -.
DR OpenTargets; ENSG00000115339; -.
DR Orphanet; 306661; Familial hyperphosphatemic tumoral calcinosis/Hyperphosphatemic hyperostosis syndrome.
DR PharmGKB; PA28538; -.
DR VEuPathDB; HostDB:ENSG00000115339; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156609; -.
DR InParanoid; Q14435; -.
DR OMA; NGEHPNL; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q14435; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q14435; -.
DR Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
DR Reactome; R-HSA-5083625; Defective GALNT3 causes HFTC.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q14435; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2591; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; GALNT3; human.
DR GeneWiki; GALNT3; -.
DR GenomeRNAi; 2591; -.
DR Pharos; Q14435; Tbio.
DR PRO; PR:Q14435; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q14435; protein.
DR Bgee; ENSG00000115339; Expressed in mucosa of sigmoid colon and 147 other tissues.
DR ExpressionAtlas; Q14435; baseline and differential.
DR Genevisible; Q14435; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IDA:BHF-UCL.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:BHF-UCL.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..633
FT /note="Polypeptide N-acetylgalactosaminyltransferase 3"
FT /id="PRO_0000059106"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..633
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 504..630
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 184..293
FT /note="Catalytic subdomain A"
FT REGION 356..418
FT /note="Catalytic subdomain B"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 401..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 517..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 561..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 605..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 173..192
FT /note="CIEQKFKRCPPLPTTSVIIV -> YVEEYLLFILYHQALQGREG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011202"
FT VAR_SEQ 193..633
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011203"
FT VARIANT 162..633
FT /note="Missing (in HFTC1)"
FT /evidence="ECO:0000269|PubMed:15133511"
FT /id="VAR_080832"
FT CONFLICT 481
FT /note="Q -> R (in Ref. 1; CAA63371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 72610 MW; 3019B2DCCC19A584 CRC64;
MAHLKRLVKL HIKRHYHKKF WKLGAVIFFF IIVLVLMQRE VSVQYSKEES RMERNMKNKN
KMLDLMLEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG YYTAAELKPV LDRPPQDSNA
PGASGKAFKT TNLSVEEQKE KERGEAKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR
CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDE YLHDKLDEYV
KQFSIVKIVR QRERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR KDETYPIKTP
TFAGGLFSIS KEYFEYIGSY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK
SPHSFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKAFGDL SKRFEIKHRL
QCKNFTWYLN NIYPEVYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL IMYTCHGLGG
NQYFEYSAQH EIRHNIQKEL CLHAAQGLVQ LKACTYKGHK TVVTGEQIWE IQKDQLLYNP
FLKMCLSANG EHPSLVSCNP SDPLQKWILS QND
