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   27-MAR-2024, entry version 214.
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   DrugBank; DB01093; Dimethyl sulfoxide.
DR   DrugCentral; Q01344; -.
DR   GuidetoPHARMACOLOGY; 1706; -.
DR   GlyCosmos; Q01344; 4 sites, No reported glycans.
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; 9606-ENSP00000412209; -.
DR   PeptideAtlas; Q01344; -.
DR   ProteomicsDB; 57939; -. [Q01344-1]
DR   ProteomicsDB; 57940; -. [Q01344-2]
DR   ProteomicsDB; 57941; -. [Q01344-3]
DR   ProteomicsDB; 5815; -.
DR   ABCD; Q01344; 1 sequenced antibody.
DR   Antibodypedia; 2274; 457 antibodies from 35 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   AGR; HGNC:6017; -.
DR   CTD; 3568; -.
DR   DisGeNET; 3568; -.
DR   GeneCards; IL5RA; -.
DR   HGNC; HGNC:6017; IL5RA.
DR   HPA; ENSG00000091181; Tissue enhanced (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; NKFRDPF; -.
DR   OrthoDB; 5301668at2759; -.
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 1141 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 111 other cell types or tissues.
DR   ExpressionAtlas; Q01344; baseline and differential.
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:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProt.
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; IDA:UniProt.
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:0038043; P:interleukin-5-mediated signaling pathway; IDA:UniProt.
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; Immunoglobulins; 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   PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR23037:SF7; INTERLEUKIN-21 RECEPTOR; 1.
DR   Pfam; PF09240; IL6Ra-bind; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
DR   Genevisible; Q01344; HS.
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;
FT                   AAA59151/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
//