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   24-JAN-2024, entry version 218.
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; DB05550; Iratumumab.
DR   DrugBank; DB06324; XmAb 2513.
DR   DrugCentral; P28908; -.
DR   GuidetoPHARMACOLOGY; 1877; -.
DR   GlyCosmos; P28908; 4 sites, No reported glycans.
DR   GlyGen; P28908; 9 sites, 1 O-linked glycan (3 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; 9606-ENSP00000263932; -.
DR   PeptideAtlas; P28908; -.
DR   ProteomicsDB; 12802; -.
DR   ProteomicsDB; 54509; -. [P28908-1]
DR   ProteomicsDB; 54510; -. [P28908-2]
DR   Pumba; P28908; -.
DR   ABCD; P28908; 25 sequenced antibodies.
DR   Antibodypedia; 3659; 2674 antibodies from 46 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   AGR; HGNC:11923; -.
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; CKACVTC; -.
DR   OrthoDB; 4050129at2759; -.
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; 22 hits in 1170 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 cell types or tissues.
DR   ExpressionAtlas; P28908; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020416; TNFR_8.
DR   InterPro; IPR034002; TNFRSF8_N.
DR   PANTHER; PTHR47497; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 8; 1.
DR   PANTHER; PTHR47497:SF1; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 8; 1.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PRINTS; PR01923; TNFACTORR8.
DR   SMART; SM00208; TNFR; 4.
DR   SUPFAM; SSF57586; TNF receptor-like; 2.
DR   PROSITE; PS00652; TNFR_NGFR_1; 2.
DR   PROSITE; PS50050; TNFR_NGFR_2; 2.
DR   Genevisible; P28908; HS.
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
//