TNR8_HUMAN
ID TNR8_HUMAN Reviewed; 595 AA.
AC P28908; B1AN79; B9EGD9; D3YTD8; Q6P4D9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 8 {ECO:0000312|HGNC:HGNC:11923};
DE AltName: Full=CD30L receptor;
DE AltName: Full=Ki-1 antigen;
DE AltName: Full=Lymphocyte activation antigen CD30;
DE AltName: CD_antigen=CD30 {ECO:0000303|PubMed:7527901};
DE Flags: Precursor;
GN Name=TNFRSF8 {ECO:0000312|HGNC:HGNC:11923};
GN Synonyms=CD30 {ECO:0000303|PubMed:7527901}, D1S166E;
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).
RC TISSUE=Lymphoid tissue;
RX PubMed=1310894; DOI=10.1016/0092-8674(92)90180-k;
RA Duerkop H., Latza U., Hummel M., Eitelbach F., Seed B., Stein H.;
RT "Molecular cloning and expression of a new member of the nerve growth
RT factor receptor family that is characteristic for Hodgkin's disease.";
RL Cell 68:421-427(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7527901; DOI=10.1016/0161-5890(94)90051-5;
RA Jung W., Krueger S., Renner C., Gause A., Sahin U., Trumper L.,
RA Pfreundschuh M.;
RT "Opposite effects of the CD30 ligand are not due to CD30 mutations: results
RT from cDNA cloning and sequence comparison of the CD30 antigen from
RT different sources.";
RL Mol. Immunol. 31:1329-1334(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=8839832;
RA Horie R., Ito K., Tatewaki M., Nagai M., Aizawa S., Higashihara M.,
RA Ishida T., Inoue J., Takizawa H., Watanabe T.;
RT "A variant CD30 protein lacking extracellular and transmembrane domains is
RT induced in HL-60 by tetradecanoylphorbol acetate and is expressed in
RT alveolar macrophages.";
RL Blood 88:2422-2432(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RC TISSUE=Placenta;
RA Durkop H., Oberbarnscheidt M., Latza U., Bulfone-Paus S.;
RT "Structure of the Hodgkin's disease associated human CD30 gene and the
RT influence of a microsatellite region on its expression in CD30+ cell
RT lines.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-273 AND GLY-402.
RG NIEHS SNPs program;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-297.
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 MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Blood, and Testis;
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8391931; DOI=10.1016/0092-8674(93)90361-s;
RA Smith C.A., Gruess H.-J., Davis T., Anderson D., Farrah T., Baker E.,
RA Sutherland G.R., Brannan C.I., Copeland N.G., Jenkins N.A., Grabstein K.H.,
RA Gliniak B., McAlister I.B., Fanslow W., Alderson M., Falk B., Gimpsel S.,
RA Gillis S., Din W.S., Goodwin R.G., Armitage R.J.;
RT "CD30 antigen, a marker for Hodgkin's lymphoma, is a receptor whose ligand
RT defines an emerging family of cytokines with homology to TNF.";
RL Cell 73:1349-1360(1993).
RN [9]
RP INTERACTION WITH TRAF1 AND TRAF2.
RX PubMed=8627180; DOI=10.1084/jem.183.2.669;
RA Lee S.Y., Park C.G., Choi Y.;
RT "T cell receptor-dependent cell death of T cell hybridomas mediated by the
RT CD30 cytoplasmic domain in association with tumor necrosis factor receptor-
RT associated factors.";
RL J. Exp. Med. 183:669-674(1996).
RN [10]
RP INTERACTION WITH TRAF3.
RX PubMed=9168896; DOI=10.1006/bbrc.1997.6509;
RA Boucher L.-M., Marengere L.E., Lu Y., Thukral S., Mak T.W.;
RT "Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other
RT members of the TNF receptor superfamily.";
RL Biochem. Biophys. Res. Commun. 233:592-600(1997).
RN [11]
RP INTERACTION WITH TRAF5.
RX PubMed=9511754; DOI=10.1016/s0378-1119(97)00616-1;
RA Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M., Otsuka M.,
RA Yamamoto T., Inoue J.;
RT "Cloning and characterization of a cDNA encoding the human homolog of tumor
RT necrosis factor receptor-associated factor 5 (TRAF5).";
RL Gene 207:135-140(1998).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TRAF5.
RX PubMed=8999898; DOI=10.1074/jbc.272.4.2042;
RA Aizawa S., Nakano H., Ishida T., Horie R., Nagai M., Ito K., Yagita H.,
RA Okumura K., Inoue J., Watanabe T.;
RT "Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2 are
RT involved in CD30-mediated NFkappaB activation.";
RL J. Biol. Chem. 272:2042-2045(1997).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 576-583 IN COMPLEX WITH TRAF2,
RP AND INTERACTION WITH TRAF2.
RX PubMed=10518213; DOI=10.1016/s1097-2765(00)80334-2;
RA Ye H., Park Y.C., Kreishman M., Kieff E., Wu H.;
RT "The structural basis for the recognition of diverse receptor sequences by
RT TRAF2.";
RL Mol. Cell 4:321-330(1999).
CC -!- FUNCTION: Receptor for TNFSF8/CD30L (PubMed:8391931). May play a role
CC in the regulation of cellular growth and transformation of activated
CC lymphoblasts. Regulates gene expression through activation of NF-kappa-
CC B (PubMed:8999898). {ECO:0000269|PubMed:8391931,
CC ECO:0000269|PubMed:8999898}.
CC -!- SUBUNIT: Interacts with TRAF1, TRAF2, TRAF3 and TRAF5.
CC {ECO:0000269|PubMed:10518213, ECO:0000269|PubMed:8627180,
CC ECO:0000269|PubMed:8999898, ECO:0000269|PubMed:9168896,
CC ECO:0000269|PubMed:9511754}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:8391931, ECO:0000305|PubMed:8999898}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:8839832}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P28908-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoplasmic, Short, C30V;
CC IsoId=P28908-2; Sequence=VSP_018900;
CC Name=3;
CC IsoId=P28908-3; Sequence=VSP_055032, VSP_055033;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Detected in alveolar macrophages (at
CC protein level). {ECO:0000269|PubMed:8839832}.
CC -!- PTM: Phosphorylated on serine and tyrosine residues (Probable). Isoform
CC 2 is constitutively phosphorylated (PubMed:8839832).
CC {ECO:0000269|PubMed:8839832, ECO:0000305}.
CC -!- MISCELLANEOUS: Most specific Hodgkin disease associated antigen.
CC -!- SIMILARITY: Belongs to the TNFR8 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf8/";
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DR EMBL; M83554; AAA51947.1; -; mRNA.
DR EMBL; S75768; AAD14188.1; -; mRNA.
DR EMBL; D86042; BAA12973.1; -; mRNA.
DR EMBL; AJ289159; CAC16652.1; -; Genomic_DNA.
DR EMBL; AY498860; AAR32099.1; -; Genomic_DNA.
DR EMBL; AL357835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063482; AAH63482.2; -; mRNA.
DR EMBL; BC136400; AAI36401.1; -; mRNA.
DR CCDS; CCDS144.1; -. [P28908-1]
DR CCDS; CCDS59989.1; -. [P28908-3]
DR PIR; A42086; A42086.
DR RefSeq; NP_001234.3; NM_001243.4. [P28908-1]
DR RefSeq; NP_001268359.2; NM_001281430.2. [P28908-3]
DR PDB; 1D01; X-ray; 2.00 A; G/H/I=576-583.
DR PDBsum; 1D01; -.
DR AlphaFoldDB; P28908; -.
DR SMR; P28908; -.
DR BioGRID; 107381; 50.
DR DIP; DIP-2930N; -.
DR ELM; P28908; -.
DR IntAct; P28908; 23.
DR STRING; 9606.ENSP00000263932; -.
DR ChEMBL; CHEMBL2364161; -.
DR DrugBank; DB08870; Brentuximab vedotin.
DR DrugBank; DB06324; XmAb 2513.
DR DrugCentral; P28908; -.
DR GuidetoPHARMACOLOGY; 1877; -.
DR GlyGen; P28908; 6 sites.
DR iPTMnet; P28908; -.
DR PhosphoSitePlus; P28908; -.
DR SwissPalm; P28908; -.
DR BioMuta; TNFRSF8; -.
DR DMDM; 115978; -.
DR EPD; P28908; -.
DR jPOST; P28908; -.
DR MassIVE; P28908; -.
DR MaxQB; P28908; -.
DR PaxDb; P28908; -.
DR PeptideAtlas; P28908; -.
DR PRIDE; P28908; -.
DR ProteomicsDB; 12802; -.
DR ProteomicsDB; 54509; -. [P28908-1]
DR ProteomicsDB; 54510; -. [P28908-2]
DR ABCD; P28908; 20 sequenced antibodies.
DR Antibodypedia; 3659; 2367 antibodies from 45 providers.
DR DNASU; 943; -.
DR Ensembl; ENST00000263932.7; ENSP00000263932.2; ENSG00000120949.15. [P28908-1]
DR Ensembl; ENST00000413146.6; ENSP00000398337.2; ENSG00000120949.15. [P28908-2]
DR Ensembl; ENST00000417814.3; ENSP00000390650.2; ENSG00000120949.15. [P28908-3]
DR GeneID; 943; -.
DR KEGG; hsa:943; -.
DR MANE-Select; ENST00000263932.7; ENSP00000263932.2; NM_001243.5; NP_001234.3.
DR UCSC; uc001atq.3; human. [P28908-1]
DR CTD; 943; -.
DR DisGeNET; 943; -.
DR GeneCards; TNFRSF8; -.
DR HGNC; HGNC:11923; TNFRSF8.
DR HPA; ENSG00000120949; Tissue enhanced (adipose).
DR MIM; 153243; gene.
DR neXtProt; NX_P28908; -.
DR OpenTargets; ENSG00000120949; -.
DR PharmGKB; PA36616; -.
DR VEuPathDB; HostDB:ENSG00000120949; -.
DR eggNOG; ENOG502SNQ9; Eukaryota.
DR GeneTree; ENSGT00510000049215; -.
DR HOGENOM; CLU_043282_0_0_1; -.
DR InParanoid; P28908; -.
DR OMA; PHTDCAK; -.
DR PhylomeDB; P28908; -.
DR TreeFam; TF331157; -.
DR PathwayCommons; P28908; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; P28908; -.
DR BioGRID-ORCS; 943; 19 hits in 1073 CRISPR screens.
DR ChiTaRS; TNFRSF8; human.
DR EvolutionaryTrace; P28908; -.
DR GeneWiki; CD30; -.
DR GenomeRNAi; 943; -.
DR Pharos; P28908; Tclin.
DR PRO; PR:P28908; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P28908; protein.
DR Bgee; ENSG00000120949; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; P28908; baseline and differential.
DR Genevisible; P28908; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032759; P:positive regulation of TRAIL production; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd13409; TNFRSF8; 2.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020416; TNFR_8.
DR InterPro; IPR034002; TNFRSF8_N.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01923; TNFACTORR8.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Cell membrane;
KW Cytoplasm; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT CHAIN 19..595
FT /note="Tumor necrosis factor receptor superfamily member 8"
FT /id="PRO_0000034573"
FT TOPO_DOM 19..385
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 28..66
FT /note="TNFR-Cys 1"
FT REPEAT 68..106
FT /note="TNFR-Cys 2"
FT REPEAT 107..150
FT /note="TNFR-Cys 3"
FT REPEAT 205..241
FT /note="TNFR-Cys 4"
FT REPEAT 243..281
FT /note="TNFR-Cys 5"
FT REPEAT 282..325
FT /note="TNFR-Cys 6"
FT REGION 167..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 45..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 48..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 69..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 84..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 87..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 108..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 131..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 233..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 244..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 259..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 262..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 283..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 289..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 1..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8839832"
FT /id="VSP_018900"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055032"
FT VAR_SEQ 446
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055033"
FT VARIANT 273
FT /note="C -> F (in dbSNP:rs2230624)"
FT /id="VAR_054213"
FT VARIANT 273
FT /note="C -> Y (in dbSNP:rs2230624)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_018753"
FT VARIANT 297
FT /note="C -> R (in dbSNP:rs1763642)"
FT /evidence="ECO:0000269|PubMed:16710414"
FT /id="VAR_055257"
FT VARIANT 314
FT /note="P -> S (in dbSNP:rs2275170)"
FT /id="VAR_055258"
FT VARIANT 402
FT /note="S -> G (in dbSNP:rs2230625)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_018754"
FT VARIANT 466
FT /note="Q -> R (in dbSNP:rs35511003)"
FT /id="VAR_055259"
SQ SEQUENCE 595 AA; 63747 MW; 7A407CC78A6E0BC8 CRC64;
MRVLLAALGL LFLGALRAFP QDRPFEDTCH GNPSHYYDKA VRRCCYRCPM GLFPTQQCPQ
RPTDCRKQCE PDYYLDEADR CTACVTCSRD DLVEKTPCAW NSSRVCECRP GMFCSTSAVN
SCARCFFHSV CPAGMIVKFP GTAQKNTVCE PASPGVSPAC ASPENCKEPS SGTIPQAKPT
PVSPATSSAS TMPVRGGTRL AQEAASKLTR APDSPSSVGR PSSDPGLSPT QPCPEGSGDC
RKQCEPDYYL DEAGRCTACV SCSRDDLVEK TPCAWNSSRT CECRPGMICA TSATNSCARC
VPYPICAAET VTKPQDMAEK DTTFEAPPLG TQPDCNPTPE NGEAPASTSP TQSLLVDSQA
SKTLPIPTSA PVALSSTGKP VLDAGPVLFW VILVLVVVVG SSAFLLCHRR ACRKRIRQKL
HLCYPVQTSQ PKLELVDSRP RRSSTQLRSG ASVTEPVAEE RGLMSQPLME TCHSVGAAYL
ESLPLQDASP AGGPSSPRDL PEPRVSTEHT NNKIEKIYIM KADTVIVGTV KAELPEGRGL
AGPAEPELEE ELEADHTPHY PEQETEPPLG SCSDVMLSVE EEGKEDPLPT AASGK
