TNR5_MOUSE
ID TNR5_MOUSE Reviewed; 289 AA.
AC P27512; Q3TS33; Q3TSL2; Q3U799; Q3U7C9; Q3UBH3; Q542B1; Q8K2X6; Q99NE0;
AC Q99NE1; Q99NE2; Q99NE3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 5;
DE AltName: Full=B-cell surface antigen CD40;
DE AltName: Full=Bp50;
DE AltName: Full=CD40L receptor;
DE AltName: CD_antigen=CD40;
DE Flags: Precursor;
GN Name=Cd40; Synonyms=Tnfrsf5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
RC STRAIN=BALB/cJ;
RX PubMed=1370315;
RA Torres R.M., Clark E.A.;
RT "Differential increase of an alternatively polyadenylated mRNA species of
RT murine CD40 upon B lymphocyte activation.";
RL J. Immunol. 148:620-626(1992).
RN [2]
RP SEQUENCE REVISION.
RA Torres R.M.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1281194;
RA Grimaldi J.C., Torres R., Kozak C.A., Chang R., Clark E.A., Howard M.,
RA Cockayne D.A.;
RT "Genomic structure and chromosomal mapping of the murine CD40 gene.";
RL J. Immunol. 149:3921-3926(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING (ISOFORMS II; III; IV
RP AND V).
RX PubMed=11172023; DOI=10.1073/pnas.98.4.1751;
RA Tone M., Tone Y., Fairchild P.J., Wykes M., Waldmann H.;
RT "Regulation of CD40 function by its isoforms generated through alternative
RT splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1751-1756(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow macrophage, Cerebellum, Colon, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 INTERACTION WITH TRAF3.
RX PubMed=7533327; DOI=10.1126/science.7533327;
RA Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.;
RT "Involvement of CRAF1, a relative of TRAF, in CD40 signaling.";
RL Science 267:1494-1498(1995).
RN [10]
RP INTERACTION WITH TRAF5.
RX PubMed=8790348; DOI=10.1073/pnas.93.18.9437;
RA Ishida T., Tojo T., Aoki T., Kobayashi N., Ohishi T., Watanabe T.,
RA Yamamoto T., Inoue J.;
RT "TRAF5, a novel tumor necrosis factor receptor-associated factor family
RT protein, mediates CD40 signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9437-9442(1996).
RN [11]
RP FUNCTION, AND INTERACTION WITH MAP3K8 AND TRAF6.
RX PubMed=12881420; DOI=10.1093/emboj/cdg386;
RA Eliopoulos A.G., Wang C.C., Dumitru C.D., Tsichlis P.N.;
RT "Tpl2 transduces CD40 and TNF signals that activate ERK and regulates IgE
RT induction by CD40.";
RL EMBO J. 22:3855-3864(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for TNFSF5/CD40LG (By similarity). Transduces
CC TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and
CC B cells, leading to induction of immunoglobulin secretion
CC (PubMed:12881420). {ECO:0000250|UniProtKB:P25942,
CC ECO:0000269|PubMed:12881420}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with TRAF1, TRAF2 and TRAF6
CC (By similarity). Interacts with TRAF3 and TRAF5. Interacts with TRAF6
CC and MAP3K8; the interaction is required for ERK activation.
CC {ECO:0000250, ECO:0000269|PubMed:12881420, ECO:0000269|PubMed:7533327,
CC ECO:0000269|PubMed:8790348}.
CC -!- INTERACTION:
CC P27512; P35991: Btk; NbExp=3; IntAct=EBI-525742, EBI-625119;
CC P27512; P39429: Traf2; NbExp=3; IntAct=EBI-525742, EBI-520016;
CC P27512; P70196: Traf6; NbExp=2; IntAct=EBI-525742, EBI-448028;
CC -!- SUBCELLULAR LOCATION: [Isoform I]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform III]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform IV]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform V]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform II]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=I;
CC IsoId=P27512-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P27512-2; Sequence=VSP_006474, VSP_006475;
CC Name=III;
CC IsoId=P27512-3; Sequence=VSP_006477, VSP_006478;
CC Name=IV;
CC IsoId=P27512-4; Sequence=VSP_006479, VSP_006480;
CC Name=V;
CC IsoId=P27512-5; Sequence=VSP_006476;
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DR EMBL; M83312; AAB08705.1; -; mRNA.
DR EMBL; M94126; AAA37404.1; -; Genomic_DNA.
DR EMBL; M94129; AAA37404.1; JOINED; Genomic_DNA.
DR EMBL; M94128; AAA37404.1; JOINED; Genomic_DNA.
DR EMBL; M94127; AAA37404.1; JOINED; Genomic_DNA.
DR EMBL; AJ401387; CAC29427.1; -; mRNA.
DR EMBL; AJ401388; CAC29428.1; -; mRNA.
DR EMBL; AJ401389; CAC29429.1; -; mRNA.
DR EMBL; AJ401390; CAC29430.1; -; mRNA.
DR EMBL; AK089861; BAC40978.1; -; mRNA.
DR EMBL; AK150959; BAE29991.1; -; mRNA.
DR EMBL; AK152716; BAE31440.1; -; mRNA.
DR EMBL; AK152756; BAE31471.1; -; mRNA.
DR EMBL; AK152942; BAE31613.1; -; mRNA.
DR EMBL; AK156644; BAE33789.1; -; mRNA.
DR EMBL; AK161978; BAE36663.1; -; mRNA.
DR EMBL; AK162305; BAE36843.1; -; mRNA.
DR EMBL; CT010343; CAJ18551.1; -; mRNA.
DR EMBL; AL591411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029254; AAH29254.1; -; mRNA.
DR CCDS; CCDS17069.1; -. [P27512-1]
DR CCDS; CCDS17070.1; -. [P27512-5]
DR CCDS; CCDS17071.1; -. [P27512-2]
DR PIR; A46476; A46476.
DR RefSeq; NP_035741.2; NM_011611.2. [P27512-1]
DR RefSeq; NP_733803.2; NM_170702.2. [P27512-5]
DR RefSeq; NP_733804.1; NM_170703.2. [P27512-2]
DR RefSeq; NP_733805.1; NM_170704.2. [P27512-4]
DR AlphaFoldDB; P27512; -.
DR SMR; P27512; -.
DR BioGRID; 204251; 18.
DR CORUM; P27512; -.
DR DIP; DIP-33295N; -.
DR ELM; P27512; -.
DR IntAct; P27512; 6.
DR MINT; P27512; -.
DR STRING; 10090.ENSMUSP00000017799; -.
DR GlyGen; P27512; 1 site.
DR iPTMnet; P27512; -.
DR PhosphoSitePlus; P27512; -.
DR SwissPalm; P27512; -.
DR EPD; P27512; -.
DR MaxQB; P27512; -.
DR PaxDb; P27512; -.
DR PeptideAtlas; P27512; -.
DR PRIDE; P27512; -.
DR ProteomicsDB; 258940; -. [P27512-1]
DR ProteomicsDB; 258941; -. [P27512-2]
DR ProteomicsDB; 258942; -. [P27512-3]
DR ProteomicsDB; 258943; -. [P27512-4]
DR ProteomicsDB; 258944; -. [P27512-5]
DR Antibodypedia; 3736; 2664 antibodies from 52 providers.
DR DNASU; 21939; -.
DR Ensembl; ENSMUST00000017799; ENSMUSP00000017799; ENSMUSG00000017652. [P27512-1]
DR Ensembl; ENSMUST00000073707; ENSMUSP00000073386; ENSMUSG00000017652. [P27512-5]
DR Ensembl; ENSMUST00000081310; ENSMUSP00000080059; ENSMUSG00000017652. [P27512-2]
DR Ensembl; ENSMUST00000184221; ENSMUSP00000139193; ENSMUSG00000017652. [P27512-3]
DR GeneID; 21939; -.
DR KEGG; mmu:21939; -.
DR UCSC; uc008nwx.1; mouse. [P27512-5]
DR UCSC; uc008nwy.1; mouse. [P27512-1]
DR UCSC; uc008nwz.1; mouse. [P27512-4]
DR UCSC; uc008nxb.1; mouse. [P27512-2]
DR CTD; 958; -.
DR MGI; MGI:88336; Cd40.
DR VEuPathDB; HostDB:ENSMUSG00000017652; -.
DR eggNOG; ENOG502S5TQ; Eukaryota.
DR GeneTree; ENSGT00940000161464; -.
DR HOGENOM; CLU_052667_4_0_1; -.
DR InParanoid; P27512; -.
DR OMA; CQPGEKL; -.
DR OrthoDB; 1038336at2759; -.
DR PhylomeDB; P27512; -.
DR TreeFam; TF331157; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR BioGRID-ORCS; 21939; 1 hit in 109 CRISPR screens.
DR PRO; PR:P27512; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P27512; protein.
DR Bgee; ENSMUSG00000017652; Expressed in peripheral lymph node and 145 other tissues.
DR ExpressionAtlas; P27512; baseline and differential.
DR Genevisible; P27512; MM.
DR GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043196; C:varicosity; ISO:MGI.
DR GO; GO:0003823; F:antigen binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0042113; P:B cell activation; IDA:MGI.
DR GO; GO:0019724; P:B cell mediated immunity; IGI:MGI.
DR GO; GO:0042100; P:B cell proliferation; IDA:MGI.
DR GO; GO:0023035; P:CD40 signaling pathway; IGI:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IDA:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IDA:MGI.
DR GO; GO:0050776; P:regulation of immune response; IDA:MGI.
DR GO; GO:0002637; P:regulation of immunoglobulin production; IDA:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IBA:GO_Central.
DR CDD; cd13407; TNFRSF5; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020435; TNFR_5.
DR InterPro; IPR034021; TNFRSF5_N.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01922; TNFACTORR5.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunity; Membrane; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..289
FT /note="Tumor necrosis factor receptor superfamily member 5"
FT /id="PRO_0000034560"
FT TOPO_DOM 20..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 25..60
FT /note="TNFR-Cys 1"
FT REPEAT 61..103
FT /note="TNFR-Cys 2"
FT REPEAT 104..144
FT /note="TNFR-Cys 3"
FT REPEAT 145..187
FT /note="TNFR-Cys 4"
FT REGION 228..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 38..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 41..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 62..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 83..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 105..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 111..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 125..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 166..203
FT /note="SCEDKNLEVLQKGTSQTNVICGLKSRMRALLVIPVVMG -> RFKVPDASPA
FT GHSCRDGHPHHHFRGVSLYQKGGQETKG (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_006474"
FT VAR_SEQ 187..216
FT /note="GLKSRMRALLVIPVVMGILITIFGVFLYIK -> E (in isoform V)"
FT /evidence="ECO:0000305"
FT /id="VSP_006476"
FT VAR_SEQ 204..289
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_006475"
FT VAR_SEQ 216..234
FT /note="KKVVKKPKDNEILPPAARR -> SECSGEEREGGFSPVEPAS (in
FT isoform III)"
FT /evidence="ECO:0000305"
FT /id="VSP_006477"
FT VAR_SEQ 216..222
FT /note="KKVVKKP -> SGQETKG (in isoform IV)"
FT /evidence="ECO:0000305"
FT /id="VSP_006479"
FT VAR_SEQ 223..289
FT /note="Missing (in isoform IV)"
FT /evidence="ECO:0000305"
FT /id="VSP_006480"
FT VAR_SEQ 235..289
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000305"
FT /id="VSP_006478"
FT CONFLICT 21
FT /note="G -> W (in Ref. 5; BAE31440)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="V -> L (in Ref. 6; CAJ18551 and 8; AAH29254)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="K -> N (in Ref. 5; BAE36843)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="T -> A (in Ref. 6; CAJ18551 and 8; AAH29254)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="A -> T (in Ref. 5; BAE29991)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="K -> E (in Ref. 5; BAE31471)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="I -> M (in Ref. 1; AAB08705, 3; AAA37404, 4;
FT CAC29430 and 5; BAC40978/BAE33789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32093 MW; C7970DAD2FEA534A CRC64;
MVSLPRLCAL WGCLLTAVHL GQCVTCSDKQ YLHDGQCCDL CQPGSRLTSH CTALEKTQCH
PCDSGEFSAQ WNREIRCHQH RHCEPNQGLR VKKEGTAESD TVCTCKEGQH CTSKDCEACA
QHTPCIPGFG VMEMATETTD TVCHPCPVGF FSNQSSLFEK CYPWTSCEDK NLEVLQKGTS
QTNVICGLKS RMRALLVIPV VMGILITIFG VFLYIKKVVK KPKDNEILPP AARRQDPQEM
EDYPGHNTAA PVQETLHGCQ PVTQEDGKES RISVQERQVT DSIALRPLV
