I12R1_HUMAN
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 03-AUG-2022, entry version 201.
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/";
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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 SMR; P42701; -.
DR BioGRID; 109808; 107.
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; 16.
DR STRING; 9606.ENSP00000470788; -.
DR ChEMBL; CHEMBL4523226; -.
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; P42701; -.
DR PeptideAtlas; P42701; -.
DR PRIDE; P42701; -.
DR ProteomicsDB; 55543; -. [P42701-1]
DR ProteomicsDB; 55544; -. [P42701-2]
DR ABCD; P42701; 2 sequenced antibodies.
DR Antibodypedia; 14966; 483 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 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; 1260765at2759; -.
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; 21 hits in 1061 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 124 other tissues.
DR ExpressionAtlas; P42701; baseline and differential.
DR Genevisible; P42701; HS.
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 interferon-gamma; IDA:BHF-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:GOC.
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:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IC:ComplexPortal.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:ComplexPortal.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:ComplexPortal.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:ComplexPortal.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:BHF-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:ComplexPortal.
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:0007165; P:signal transduction; IC:BHF-UCL.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
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
