ID I12R1_HUMAN Reviewed; 662 AA. AC P42701; A8K308; B2RPF1; B7ZKK3; Q8N6Q7; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Interleukin-12 receptor subunit beta-1; DE Short=IL-12 receptor subunit beta-1; DE Short=IL-12R subunit beta-1; DE Short=IL-12R-beta-1; DE Short=IL-12RB1; DE AltName: Full=IL-12 receptor beta component; DE AltName: CD_antigen=CD212; DE Flags: Precursor; GN Name=IL12RB1; Synonyms=IL12R, IL12RB; 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 2). RX PubMed=7911493; RA Chua A.O., Chizzonite R., Desai B.B., Truitt T.P., Nunes P., Minetti L.J., RA Warrier R.R., Presky D.H., Levine J.F., Gately M.K., Gubler U.; RT "Expression cloning of a human IL-12 receptor component. A new member of RT the cytokine receptor superfamily with strong homology to gp130."; RL J. Immunol. 153:128-136(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Elloumi-Zghal H., Abdelhak S., Dellagi K.; RT "Genomic structure of IL12RB1 gene."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-3; SER-47; HIS-156; RP ARG-214; GLN-339; THR-365 AND ARG-378. RG SeattleSNPs variation discovery resource; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP ARG-214. RC TISSUE=Colon, 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 SUBUNIT. RX PubMed=8943050; DOI=10.1073/pnas.93.24.14002; RA Presky D.H., Yang H., Minetti L.J., Chua A.O., Nabavi N., Wu C.-Y., RA Gately M.K., Gubler U.; RT "A functional interleukin 12 receptor complex is composed of two beta-type RT cytokine receptor subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 93:14002-14007(1996). RN [9] RP FUNCTION, AND INTERACTION WITH IL23R. RX PubMed=12023369; DOI=10.4049/jimmunol.168.11.5699; RA Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J., RA Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J., RA O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D., RA Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.; RT "A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 RT and a novel cytokine receptor subunit, IL-23R."; RL J. Immunol. 168:5699-5708(2002). RN [10] RP VARIANT IMD30 TRP-213. RX PubMed=11424023; DOI=10.1086/321999; RA Altare F., Ensser A., Breiman A., Reichenbach J., El Baghdadi J., RA Fischer A., Emile J.-F., Gaillard J.-L., Meinl E., Casanova J.-L.; RT "Interleukin-12 receptor beta-1 deficiency in a patient with abdominal RT tuberculosis."; RL J. Infect. Dis. 184:231-236(2001). CC -!- FUNCTION: Functions as an interleukin receptor which binds interleukin- CC 12 with low affinity and is involved in IL12 transduction. Associated CC with IL12RB2 it forms a functional, high affinity receptor for IL12. CC Associates also with IL23R to form the interleukin-23 receptor which CC functions in IL23 signal transduction probably through activation of CC the Jak-Stat signaling cascade. {ECO:0000269|PubMed:12023369}. CC -!- SUBUNIT: Dimer or oligomer; disulfide-linked. Interacts with IL12RB2 to CC form the high affinity IL12 receptor. Heterodimer with IL23R; in CC presence of IL23. The heterodimer forms the IL23 receptor. CC {ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:8943050}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Long; CC IsoId=P42701-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P42701-2; Sequence=VSP_001715; CC Name=3; CC IsoId=P42701-3; Sequence=VSP_037043, VSP_037044; CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein CC folding and thereby efficient intracellular transport and cell-surface CC receptor binding. CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or CC activation. CC -!- DISEASE: Immunodeficiency 30 (IMD30) [MIM:614891]: A form of Mendelian CC susceptibility to mycobacterial disease, a rare condition caused by CC impairment of interferon-gamma mediated immunity. It is characterized CC by predisposition to illness caused by moderately virulent CC mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, CC environmental non-tuberculous mycobacteria, and by the more virulent CC Mycobacterium tuberculosis. Other microorganisms rarely cause severe CC clinical disease in individuals with susceptibility to mycobacterial CC infections, with the exception of Salmonella which infects less than CC 50% of these individuals. Clinical outcome severity depends on the CC degree of impairment of interferon-gamma mediated immunity. Some CC patients die of overwhelming mycobacterial disease with lepromatous- CC like lesions in early childhood, whereas others develop, later in life, CC disseminated but curable infections with tuberculoid granulomas. IMD30 CC has low penetrance, and affected individuals have relatively mild CC disease and good prognosis. BCG disease and salmonellosis are the most CC frequent infections in IMD30 patients. {ECO:0000269|PubMed:11424023}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=IL12RB1base; Note=IL12RB1 mutation db; CC URL="http://structure.bmc.lu.se/idbase/IL12RB1base/"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/il12rb1/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U03187; AAA21340.1; -; mRNA. DR EMBL; AJ297688; CAC10446.1; -; Genomic_DNA. DR EMBL; AJ297689; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297690; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297691; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297692; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297693; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297694; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297695; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297696; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297697; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297698; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297699; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297700; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AJ297701; CAC10446.1; JOINED; Genomic_DNA. DR EMBL; AY771996; AAV28734.1; -; Genomic_DNA. DR EMBL; AK290423; BAF83112.1; -; mRNA. DR EMBL; AC020904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84656.1; -; Genomic_DNA. DR EMBL; BC029121; AAH29121.1; -; mRNA. DR EMBL; BC137404; AAI37405.1; -; mRNA. DR EMBL; BC137406; AAI37407.1; -; mRNA. DR CCDS; CCDS32957.1; -. [P42701-3] DR CCDS; CCDS54232.1; -. [P42701-1] DR PIR; I37892; I37892. DR RefSeq; NP_001276952.1; NM_001290023.1. [P42701-2] DR RefSeq; NP_005526.1; NM_005535.2. [P42701-1] DR RefSeq; NP_714912.1; NM_153701.2. [P42701-3] DR PDB; 6WDP; X-ray; 2.01 A; A=27-239. DR PDB; 6WDQ; X-ray; 3.40 A; D=27-239. DR PDBsum; 6WDP; -. DR PDBsum; 6WDQ; -. DR AlphaFoldDB; P42701; -. DR EMDB; EMD-21645; -. DR EMDB; EMD-21646; -. DR SMR; P42701; -. DR BioGRID; 109808; 109. DR ComplexPortal; CPX-382; Interleukin-12-receptor complex. DR ComplexPortal; CPX-383; Interleukin-23-receptor complex. DR CORUM; P42701; -. DR DIP; DIP-3773N; -. DR IntAct; P42701; 17. DR MINT; P42701; -. DR STRING; 9606.ENSP00000470788; -. DR ChEMBL; CHEMBL4523226; -. DR GlyCosmos; P42701; 6 sites, No reported glycans. DR GlyGen; P42701; 6 sites. DR iPTMnet; P42701; -. DR PhosphoSitePlus; P42701; -. DR BioMuta; IL12RB1; -. DR DMDM; 1170462; -. DR MassIVE; P42701; -. DR MaxQB; P42701; -. DR PaxDb; 9606-ENSP00000470788; -. DR PeptideAtlas; P42701; -. DR ProteomicsDB; 55543; -. [P42701-1] DR ProteomicsDB; 55544; -. [P42701-2] DR ABCD; P42701; 2 sequenced antibodies. DR Antibodypedia; 14966; 555 antibodies from 40 providers. DR DNASU; 3594; -. DR Ensembl; ENST00000322153.11; ENSP00000314425.5; ENSG00000096996.16. [P42701-3] DR Ensembl; ENST00000593993.7; ENSP00000472165.2; ENSG00000096996.16. [P42701-1] DR Ensembl; ENST00000600835.6; ENSP00000470788.1; ENSG00000096996.16. [P42701-1] DR GeneID; 3594; -. DR KEGG; hsa:3594; -. DR MANE-Select; ENST00000593993.7; ENSP00000472165.2; NM_005535.3; NP_005526.1. DR UCSC; uc002nhw.2; human. [P42701-1] DR AGR; HGNC:5971; -. DR CTD; 3594; -. DR DisGeNET; 3594; -. DR GeneCards; IL12RB1; -. DR HGNC; HGNC:5971; IL12RB1. DR HPA; ENSG00000096996; Tissue enhanced (lymphoid). DR MalaCards; IL12RB1; -. DR MIM; 601604; gene. DR MIM; 614891; phenotype. DR neXtProt; NX_P42701; -. DR OpenTargets; ENSG00000096996; -. DR Orphanet; 319552; Mendelian susceptibility to mycobacterial diseases due to complete IL12RB1 deficiency. DR Orphanet; 186; Primary biliary cholangitis. DR PharmGKB; PA29786; -. DR VEuPathDB; HostDB:ENSG00000096996; -. DR eggNOG; ENOG502S2KP; Eukaryota. DR GeneTree; ENSGT00390000012431; -. DR HOGENOM; CLU_031440_0_0_1; -. DR InParanoid; P42701; -. DR OMA; ECSWEYE; -. DR OrthoDB; 5302074at2759; -. DR PhylomeDB; P42701; -. DR TreeFam; TF338613; -. DR PathwayCommons; P42701; -. DR Reactome; R-HSA-9020591; Interleukin-12 signaling. DR Reactome; R-HSA-9020933; Interleukin-23 signaling. DR SignaLink; P42701; -. DR SIGNOR; P42701; -. DR BioGRID-ORCS; 3594; 24 hits in 1139 CRISPR screens. DR ChiTaRS; IL12RB1; human. DR GeneWiki; Interleukin_12_receptor,_beta_1_subunit; -. DR GenomeRNAi; 3594; -. DR Pharos; P42701; Tbio. DR PRO; PR:P42701; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P42701; Protein. DR Bgee; ENSG00000096996; Expressed in granulocyte and 125 other cell types or tissues. DR ExpressionAtlas; P42701; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0042022; C:interleukin-12 receptor complex; IDA:BHF-UCL. DR GO; GO:0072536; C:interleukin-23 receptor complex; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central. DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:BHF-UCL. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IDA:UniProt. DR GO; GO:0038155; P:interleukin-23-mediated signaling pathway; IEA:GOC. DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL. DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:BHF-UCL. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IDA:BHF-UCL. DR GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; ISS:BHF-UCL. DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:BHF-UCL. DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:BHF-UCL. DR GO; GO:0007165; P:signal transduction; IC:BHF-UCL. DR CDD; cd00063; FN3; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1. DR PANTHER; PTHR23036:SF51; INTERLEUKIN-12 RECEPTOR SUBUNIT BETA-1; 1. DR Pfam; PF00041; fn3; 1. DR SMART; SM00060; FN3; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1. DR Genevisible; P42701; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond; KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..662 FT /note="Interleukin-12 receptor subunit beta-1" FT /id="PRO_0000010917" FT TOPO_DOM 24..545 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 546..570 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 571..662 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 46..136 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 142..234 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 237..337 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 338..444 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 448..542 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 626..648 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 222..226 FT /note="WSXWS motif" FT MOTIF 577..585 FT /note="Box 1 motif" FT CARBOHYD 121 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 352 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 442 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 52..62 FT /evidence="ECO:0000250" FT VAR_SEQ 341..422 FT /note="EPVALNISVGTNGTTMYWPARAQSMTYCIEWQPVGQDGGLATCSLTAPQDPD FT PAGMATYSWSRESGAMGQEKCYYITIFASA -> DGMISAHCNLRLPDSRDSPASASRV FT AGITGICHHTRLILYF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_037043" FT VAR_SEQ 423..662 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_037044" FT VAR_SEQ 659..662 FT /note="KAKM -> DR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7911493" FT /id="VSP_001715" FT VARIANT 3 FT /note="P -> Q (in dbSNP:rs17884651)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021281" FT VARIANT 47 FT /note="P -> S (in dbSNP:rs17887176)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021282" FT VARIANT 156 FT /note="R -> H (in dbSNP:rs11575926)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021283" FT VARIANT 213 FT /note="R -> W (in IMD30; dbSNP:rs121434494)" FT /evidence="ECO:0000269|PubMed:11424023" FT /id="VAR_015577" FT VARIANT 214 FT /note="Q -> R (in dbSNP:rs11575934)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_021284" FT VARIANT 339 FT /note="H -> Q (in dbSNP:rs17884957)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_021285" FT VARIANT 365 FT /note="M -> T (in dbSNP:rs375947)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_011986" FT VARIANT 378 FT /note="G -> R (in dbSNP:rs401502)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_011987" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 56..68 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 74..80 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 107..119 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:6WDP" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 167..175 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 191..199 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 206..214 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:6WDP" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:6WDP" SQ SEQUENCE 662 AA; 73109 MW; 541ADA60F62DA1EF CRC64; MEPLVTWVVP LLFLFLLSRQ GAACRTSECC FQDPPYPDAD SGSASGPRDL RCYRISSDRY ECSWQYEGPT AGVSHFLRCC LSSGRCCYFA AGSATRLQFS DQAGVSVLYT VTLWVESWAR NQTEKSPEVT LQLYNSVKYE PPLGDIKVSK LAGQLRMEWE TPDNQVGAEV QFRHRTPSSP WKLGDCGPQD DDTESCLCPL EMNVAQEFQL RRRQLGSQGS SWSKWSSPVC VPPENPPQPQ VRFSVEQLGQ DGRRRLTLKE QPTQLELPEG CQGLAPGTEV TYRLQLHMLS CPCKAKATRT LHLGKMPYLS GAAYNVAVIS SNQFGPGLNQ TWHIPADTHT EPVALNISVG TNGTTMYWPA RAQSMTYCIE WQPVGQDGGL ATCSLTAPQD PDPAGMATYS WSRESGAMGQ EKCYYITIFA SAHPEKLTLW STVLSTYHFG GNASAAGTPH HVSVKNHSLD SVSVDWAPSL LSTCPGVLKE YVVRCRDEDS KQVSEHPVQP TETQVTLSGL RAGVAYTVQV RADTAWLRGV WSQPQRFSIE VQVSDWLIFF ASLGSFLSIL LVGVLGYLGL NRAARHLCPP LPTPCASSAI EFPGGKETWQ WINPVDFQEE ASLQEALVVE MSWDKGERTE PLEKTELPEG APELALDTEL SLEDGDRCKA KM //