IL5RA_HUMAN
ID IL5RA_HUMAN Reviewed; 420 AA.
AC Q01344; B3IU77; B4E2G0; Q14633; Q15469; Q6ISX9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Interleukin-5 receptor subunit alpha;
DE Short=IL-5 receptor subunit alpha;
DE Short=IL-5R subunit alpha;
DE Short=IL-5R-alpha;
DE Short=IL-5RA;
DE AltName: Full=CDw125;
DE AltName: CD_antigen=CD125;
DE Flags: Precursor;
GN Name=IL5RA; Synonyms=IL5R;
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 2).
RX PubMed=1833065; DOI=10.1016/0092-8674(91)90040-6;
RA Tavernier J., Devos R., Cornelis S., Tuypens T., van der Heyden J.,
RA Fiers W., Plaetinck G.;
RT "A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-
RT specific alpha chain and a beta chain shared with the receptor for GM-
RT CSF.";
RL Cell 66:1175-1184(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND VARIANT VAL-129.
RC TISSUE=Peripheral blood;
RX PubMed=1732409; DOI=10.1084/jem.175.2.341;
RA Murata Y., Takaki S., Migita M., Kikuchi Y., Tominaga A., Takatsu K.;
RT "Molecular cloning and expression of the human interleukin 5 receptor.";
RL J. Exp. Med. 175:341-351(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH IL5 AND
RP CSF2RB, AND FUNCTION.
RX PubMed=1495999; DOI=10.1073/pnas.89.15.7041;
RA Tavernier J., Tuypens T., Plaetinck G., Verhee A., Fiers W., Devos R.;
RT "Molecular basis of the membrane-anchored and two soluble isoforms of the
RT human interleukin 5 receptor alpha subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7041-7045(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Ishihara K., Yamada M., Hirasawa N., Ohuchi K.;
RT "Isolation of the variants for human interleukin-5 receptor alpha
RT subunit.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-129 AND ALA-262.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP FUNCTION.
RX PubMed=9378992;
RA Monahan J., Siegel N., Keith R., Caparon M., Christine L., Compton R.,
RA Cusik S., Hirsch J., Huynh M., Devine C., Polazzi J., Rangwala S., Tsai B.,
RA Portanova J.;
RT "Attenuation of IL-5-mediated signal transduction, eosinophil survival, and
RT inflammatory mediator release by a soluble human IL-5 receptor.";
RL J. Immunol. 159:4024-4034(1997).
RN [9]
RP FUNCTION, AND INTERACTION WITH CSF2RB AND JAK2.
RX PubMed=9516124;
RA Ogata N., Kouro T., Yamada A., Koike M., Hanai N., Ishikawa T., Takatsu K.;
RT "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5)
RT receptor alpha and betac subunit, respectively, and are activated upon IL-5
RT stimulation.";
RL Blood 91:2264-2271(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-420 IN COMPLEX WITH SDCBP.
RX PubMed=12842047; DOI=10.1016/s0969-2126(03)00125-4;
RA Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.;
RT "Molecular roots of degenerate specificity in syntenin's PDZ2 domain:
RT reassessment of the PDZ recognition paradigm.";
RL Structure 11:845-853(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 20-332 IN COMPLEX WITH IL5, AND
RP DISULFIDE BONDS.
RX PubMed=22153509; DOI=10.1016/j.str.2011.08.015;
RA Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W.,
RA Mueller T.D.;
RT "Structure analysis of the IL-5 ligand-receptor complex reveals a wrench-
RT like architecture for IL-5Ralpha.";
RL Structure 19:1864-1875(2011).
RN [12] {ECO:0007744|PDB:3VA2}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 23-134 IN COMPLEX WITH IL5,
RP SUBUNIT, AND FUNCTION.
RX PubMed=22528658; DOI=10.1002/pro.2072;
RA Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Ikutani M., Takaki S.,
RA Sakamoto K., Hara-Yokoyama M., Shirouzu M., Takatsu K., Yokoyama S.;
RT "Structural basis of interleukin-5 dimer recognition by its alpha
RT receptor.";
RL Protein Sci. 21:850-864(2012).
CC -!- FUNCTION: Cell surface receptor that plays an important role in the
CC survival, differentiation, and chemotaxis of eosinophils
CC (PubMed:9378992). Acts by forming an heterodimeric receptor with CSF2RB
CC subunit and subsequently binding to interleukin-5 (PubMed:1495999,
CC PubMed:22528658). In unstimulated conditions, interacts constitutively
CC with JAK2. Heterodimeric receptor activation leads to JAK2 stimulation
CC and subsequent activation of the JAK-STAT pathway (PubMed:9516124).
CC {ECO:0000269|PubMed:1495999, ECO:0000269|PubMed:22528658,
CC ECO:0000269|PubMed:9378992, ECO:0000269|PubMed:9516124}.
CC -!- SUBUNIT: Interacts with IL5 (PubMed:1495999, PubMed:22153509,
CC PubMed:22528658). Interacts with CSF2RB (PubMed:9516124). Interacts
CC with JAK2 (PubMed:9516124). Interacts with SDCBP (PubMed:12842047).
CC {ECO:0000269|PubMed:12842047, ECO:0000269|PubMed:1495999,
CC ECO:0000269|PubMed:22153509, ECO:0000269|PubMed:22528658}.
CC -!- INTERACTION:
CC Q01344; P32927: CSF2RB; NbExp=3; IntAct=EBI-1759442, EBI-1809771;
CC Q01344; P05113: IL5; NbExp=2; IntAct=EBI-1759442, EBI-2435811;
CC Q01344; O60674: JAK2; NbExp=2; IntAct=EBI-1759442, EBI-518647;
CC Q01344; O00560: SDCBP; NbExp=2; IntAct=EBI-1759442, EBI-727004;
CC Q01344-2; P05113: IL5; NbExp=4; IntAct=EBI-15957545, EBI-2435811;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Membrane-bound;
CC IsoId=Q01344-1; Sequence=Displayed;
CC Name=2; Synonyms=Soluble-S1;
CC IsoId=Q01344-2; Sequence=VSP_001678, VSP_001679;
CC Name=3; Synonyms=Soluble-S2;
CC IsoId=Q01344-3; Sequence=VSP_001680, VSP_001681;
CC Name=4;
CC IsoId=Q01344-4; Sequence=VSP_046742;
CC Name=5;
CC IsoId=Q01344-5; Sequence=VSP_047762;
CC -!- TISSUE SPECIFICITY: Expressed on eosinophils and basophils.
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 -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il5ra/";
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DR EMBL; M75914; AAA36110.1; -; mRNA.
DR EMBL; X61176; CAA43483.1; -; mRNA.
DR EMBL; X62156; CAA44081.1; -; mRNA.
DR EMBL; M96651; AAA59151.1; -; mRNA.
DR EMBL; M96652; AAA59152.1; -; mRNA.
DR EMBL; AB288090; BAG49562.1; -; mRNA.
DR EMBL; AK304256; BAG65122.1; -; mRNA.
DR EMBL; AY642135; AAT45457.1; -; Genomic_DNA.
DR EMBL; AC022002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS2559.1; -. [Q01344-1]
DR CCDS; CCDS2560.1; -. [Q01344-2]
DR CCDS; CCDS46739.1; -. [Q01344-3]
DR CCDS; CCDS58813.1; -. [Q01344-4]
DR PIR; A40267; A40267.
DR RefSeq; NP_000555.2; NM_000564.4. [Q01344-1]
DR RefSeq; NP_001230028.1; NM_001243099.1. [Q01344-4]
DR RefSeq; NP_783851.1; NM_175724.2. [Q01344-3]
DR RefSeq; NP_783852.1; NM_175725.2. [Q01344-2]
DR RefSeq; NP_783853.1; NM_175726.3. [Q01344-1]
DR RefSeq; NP_783854.1; NM_175727.2. [Q01344-3]
DR RefSeq; NP_783855.1; NM_175728.2. [Q01344-2]
DR PDB; 1OBX; X-ray; 1.35 A; B=413-420.
DR PDB; 1OBZ; X-ray; 1.69 A; P=413-420.
DR PDB; 3QT2; X-ray; 2.55 A; A/B=20-335.
DR PDB; 3VA2; X-ray; 2.70 A; C=21-335.
DR PDB; 6H41; X-ray; 2.75 A; A=27-332.
DR PDBsum; 1OBX; -.
DR PDBsum; 1OBZ; -.
DR PDBsum; 3QT2; -.
DR PDBsum; 3VA2; -.
DR PDBsum; 6H41; -.
DR AlphaFoldDB; Q01344; -.
DR SMR; Q01344; -.
DR BioGRID; 109782; 143.
DR DIP; DIP-3510N; -.
DR ELM; Q01344; -.
DR IntAct; Q01344; 6.
DR STRING; 9606.ENSP00000412209; -.
DR ChEMBL; CHEMBL3580483; -.
DR DrugBank; DB12023; Benralizumab.
DR DrugCentral; Q01344; -.
DR GuidetoPHARMACOLOGY; 1706; -.
DR GlyGen; Q01344; 4 sites.
DR iPTMnet; Q01344; -.
DR PhosphoSitePlus; Q01344; -.
DR BioMuta; IL5RA; -.
DR DMDM; 116242525; -.
DR MassIVE; Q01344; -.
DR MaxQB; Q01344; -.
DR PaxDb; Q01344; -.
DR PeptideAtlas; Q01344; -.
DR PRIDE; Q01344; -.
DR ABCD; Q01344; 1 sequenced antibody.
DR Antibodypedia; 2274; 413 antibodies from 34 providers.
DR DNASU; 3568; -.
DR Ensembl; ENST00000256452.7; ENSP00000256452.3; ENSG00000091181.20. [Q01344-1]
DR Ensembl; ENST00000311981.12; ENSP00000309196.8; ENSG00000091181.20. [Q01344-2]
DR Ensembl; ENST00000383846.5; ENSP00000373358.1; ENSG00000091181.20. [Q01344-2]
DR Ensembl; ENST00000430514.6; ENSP00000400400.2; ENSG00000091181.20. [Q01344-3]
DR Ensembl; ENST00000438560.5; ENSP00000390753.1; ENSG00000091181.20. [Q01344-4]
DR Ensembl; ENST00000446632.7; ENSP00000412209.2; ENSG00000091181.20. [Q01344-1]
DR Ensembl; ENST00000456302.5; ENSP00000392059.1; ENSG00000091181.20. [Q01344-3]
DR GeneID; 3568; -.
DR KEGG; hsa:3568; -.
DR MANE-Select; ENST00000446632.7; ENSP00000412209.2; NM_175726.4; NP_783853.1.
DR UCSC; uc010hbs.4; human. [Q01344-1]
DR CTD; 3568; -.
DR DisGeNET; 3568; -.
DR GeneCards; IL5RA; -.
DR HGNC; HGNC:6017; IL5RA.
DR HPA; ENSG00000091181; Tissue enhanced (brain, choroid plexus, fallopian tube).
DR MIM; 147851; gene.
DR neXtProt; NX_Q01344; -.
DR OpenTargets; ENSG00000091181; -.
DR PharmGKB; PA29834; -.
DR VEuPathDB; HostDB:ENSG00000091181; -.
DR eggNOG; ENOG502QZNV; Eukaryota.
DR GeneTree; ENSGT00940000160890; -.
DR HOGENOM; CLU_039945_0_0_1; -.
DR InParanoid; Q01344; -.
DR OMA; HAIDQVN; -.
DR OrthoDB; 1151666at2759; -.
DR PhylomeDB; Q01344; -.
DR TreeFam; TF331549; -.
DR PathwayCommons; Q01344; -.
DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR SignaLink; Q01344; -.
DR SIGNOR; Q01344; -.
DR BioGRID-ORCS; 3568; 9 hits in 1061 CRISPR screens.
DR ChiTaRS; IL5RA; human.
DR EvolutionaryTrace; Q01344; -.
DR GeneWiki; Interleukin_5_receptor_alpha_subunit; -.
DR GenomeRNAi; 3568; -.
DR Pharos; Q01344; Tclin.
DR PRO; PR:Q01344; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q01344; protein.
DR Bgee; ENSG00000091181; Expressed in right uterine tube and 110 other tissues.
DR ExpressionAtlas; Q01344; baseline and differential.
DR Genevisible; Q01344; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
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:0004914; F:interleukin-5 receptor activity; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; TAS:GO_Central.
DR GO; GO:0032674; P:regulation of interleukin-5 production; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT CHAIN 21..420
FT /note="Interleukin-5 receptor subunit alpha"
FT /id="PRO_0000010893"
FT TOPO_DOM 21..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..123
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 241..334
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 322..326
FT /note="WSXWS motif"
FT MOTIF 371..379
FT /note="Box 1 motif"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..155
FT /evidence="ECO:0000269|PubMed:22153509"
FT DISULFID 182..196
FT /evidence="ECO:0000269|PubMed:22153509"
FT DISULFID 269..316
FT /evidence="ECO:0000269|PubMed:22153509"
FT VAR_SEQ 123..331
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047762"
FT VAR_SEQ 333..335
FT /note="NDE -> FSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1833065"
FT /id="VSP_001678"
FT VAR_SEQ 333
FT /note="N -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1495999,
FT ECO:0000303|PubMed:1732409"
FT /id="VSP_001680"
FT VAR_SEQ 334..420
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1495999,
FT ECO:0000303|PubMed:1732409"
FT /id="VSP_001681"
FT VAR_SEQ 336..420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1833065"
FT /id="VSP_001679"
FT VAR_SEQ 365..420
FT /note="CHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVICYIEKPGVETLE
FT DSVF -> KLGPVRRKLKSSVI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046742"
FT VARIANT 129
FT /note="I -> V (in dbSNP:rs2290610)"
FT /evidence="ECO:0000269|PubMed:1732409, ECO:0000269|Ref.6"
FT /id="VAR_020654"
FT VARIANT 262
FT /note="V -> A (in dbSNP:rs17879690)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_020655"
FT CONFLICT 212
FT /note="A -> S (in Ref. 1; AAA36110 and 2; AAA59151/
FT AAA59152)"
FT /evidence="ECO:0000305"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6H41"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 75..87
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3VA2"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6H41"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6H41"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:3QT2"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3QT2"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:3QT2"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 284..297
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:3QT2"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3QT2"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3QT2"
SQ SEQUENCE 420 AA; 47685 MW; 4E0A5F2838B9C4FE CRC64;
MIIVAHVLLI LLGATEILQA DLLPDEKISL LPPVNFTIKV TGLAQVLLQW KPNPDQEQRN
VNLEYQVKIN APKEDDYETR ITESKCVTIL HKGFSASVRT ILQNDHSLLA SSWASAELHA
PPGSPGTSIV NLTCTTNTTE DNYSRLRSYQ VSLHCTWLVG TDAPEDTQYF LYYRYGSWTE
ECQEYSKDTL GRNIACWFPR TFILSKGRDW LAVLVNGSSK HSAIRPFDQL FALHAIDQIN
PPLNVTAEIE GTRLSIQWEK PVSAFPIHCF DYEVKIHNTR NGYLQIEKLM TNAFISIIDD
LSKYDVQVRA AVSSMCREAG LWSEWSQPIY VGNDEHKPLR EWFVIVIMAT ICFILLILSL
ICKICHLWIK LFPPIPAPKS NIKDLFVTTN YEKAGSSETE IEVICYIEKP GVETLEDSVF
