I13R1_HUMAN
ID I13R1_HUMAN Reviewed; 427 AA.
AC P78552; O95646; Q5JSL4; Q99656; Q9UDY5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Interleukin-13 receptor subunit alpha-1;
DE Short=IL-13 receptor subunit alpha-1;
DE Short=IL-13R subunit alpha-1;
DE Short=IL-13R-alpha-1;
DE Short=IL-13RA1;
DE AltName: Full=Cancer/testis antigen 19;
DE Short=CT19;
DE AltName: CD_antigen=CD213a1;
DE Flags: Precursor;
GN Name=IL13RA1; Synonyms=IL13R, IL13RA;
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 1).
RC TISSUE=Carcinoma;
RX PubMed=9013879; DOI=10.1016/s0014-5793(96)01462-7;
RA Miloux B., Laurent P., Bonnin O., Lupker J., Caput D., Vita N., Ferrara P.;
RT "Cloning of the human IL-13R alpha1 chain and reconstitution with the IL4R
RT alpha of a functional IL-4/IL-13 receptor complex.";
RL FEBS Lett. 401:163-166(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RA Gauchat J.-F., Schlagenhauf E., Feng N.P., Moser R., Yamage M., Jeannin P.,
RA Alouani S., Elson G., Notarangelo L.D., Wells T., Eugster H.P.,
RA Bonnefoy J.-Y.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=8910586; DOI=10.1074/jbc.271.46.29265;
RA Aman M.J., Tayebi N., Obiri N.I., Puri R.K., Modi W.S., Leonard W.J.;
RT "cDNA cloning and characterization of the human interleukin 13 receptor
RT alpha chain.";
RL J. Biol. Chem. 271:29265-29270(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Wada M., Hisano T., Kuwano M.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 TRAF3IP1.
RX PubMed=10791955; DOI=10.1074/jbc.m001095200;
RA Ling L., Goeddel D.V.;
RT "MIP-T3, a novel protein linking tumor necrosis factor receptor-associated
RT factor 3 to the microtubule network.";
RL J. Biol. Chem. 275:23852-23860(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-342 IN COMPLEXES WITH IL4;
RP IL4RA AND IL13, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=18243101; DOI=10.1016/j.cell.2007.12.030;
RA LaPorte S.L., Juo Z.S., Vaclavikova J., Colf L.A., Qi X., Heller N.M.,
RA Keegan A.D., Garcia K.C.;
RT "Molecular and structural basis of cytokine receptor pleiotropy in the
RT interleukin-4/13 system.";
RL Cell 132:259-272(2008).
CC -!- FUNCTION: Binds with low affinity to interleukin-13 (IL13). Together
CC with IL4RA can form a functional receptor for IL13. Also serves as an
CC alternate accessory protein to the common cytokine receptor gamma chain
CC for interleukin-4 (IL4) signaling, but cannot replace the function of
CC IL2RG in allowing enhanced interleukin-2 (IL2) binding activity.
CC -!- SUBUNIT: Interleukin-13 receptor is a complex of IL4R, IL13RA1, and
CC possibly other components. Interacts with TRAF3IP1. Interacts with IL4
CC (PubMed:18243101). {ECO:0000269|PubMed:10791955,
CC ECO:0000269|PubMed:18243101}.
CC -!- INTERACTION:
CC P78552; P35225: IL13; NbExp=6; IntAct=EBI-1391535, EBI-1647828;
CC P78552; P05112: IL4; NbExp=3; IntAct=EBI-1391535, EBI-367025;
CC P78552; Q8TDR0: TRAF3IP1; NbExp=3; IntAct=EBI-1391535, EBI-928811;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P78552-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78552-2; Sequence=VSP_055587, VSP_055588;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in heart, liver,
CC skeletal muscle and ovary; lowest levels in brain, lung and kidney.
CC Also found in B-cells, T-cells and endothelial cells.
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}.
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DR EMBL; Y10659; CAA71669.1; -; mRNA.
DR EMBL; Y09328; CAA70508.1; -; mRNA.
DR EMBL; U62858; AAB37127.1; -; mRNA.
DR EMBL; U81379; AAD00510.3; -; mRNA.
DR EMBL; U81380; AAD00511.2; -; mRNA.
DR EMBL; AK313467; BAG36253.1; -; mRNA.
DR EMBL; AL391280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471161; EAW89893.1; -; Genomic_DNA.
DR EMBL; BC009960; AAH09960.1; -; mRNA.
DR CCDS; CCDS14573.1; -. [P78552-1]
DR RefSeq; NP_001551.1; NM_001560.2. [P78552-1]
DR PDB; 3BPN; X-ray; 3.02 A; C=29-342.
DR PDB; 3BPO; X-ray; 3.00 A; C=29-342.
DR PDB; 4HWB; X-ray; 2.61 A; A=223-336.
DR PDB; 5E4E; X-ray; 3.00 A; C=23-340.
DR PDBsum; 3BPN; -.
DR PDBsum; 3BPO; -.
DR PDBsum; 4HWB; -.
DR PDBsum; 5E4E; -.
DR AlphaFoldDB; P78552; -.
DR SMR; P78552; -.
DR BioGRID; 109811; 19.
DR CORUM; P78552; -.
DR DIP; DIP-3225N; -.
DR IntAct; P78552; 13.
DR STRING; 9606.ENSP00000360730; -.
DR ChEMBL; CHEMBL3831285; -.
DR GuidetoPHARMACOLOGY; 1700; -.
DR TCDB; 8.A.152.1.9; the interleukin receptor (ilr) family.
DR GlyConnect; 2052; 1 N-Linked glycan (1 site).
DR GlyGen; P78552; 11 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P78552; -.
DR PhosphoSitePlus; P78552; -.
DR BioMuta; IL13RA1; -.
DR DMDM; 2494718; -.
DR EPD; P78552; -.
DR jPOST; P78552; -.
DR MassIVE; P78552; -.
DR PaxDb; P78552; -.
DR PeptideAtlas; P78552; -.
DR PRIDE; P78552; -.
DR ProteomicsDB; 57649; -. [P78552-1]
DR ProteomicsDB; 84133; -.
DR ABCD; P78552; 17 sequenced antibodies.
DR Antibodypedia; 385; 562 antibodies from 36 providers.
DR DNASU; 3597; -.
DR Ensembl; ENST00000371642.1; ENSP00000360705.1; ENSG00000131724.11. [P78552-2]
DR Ensembl; ENST00000371666.8; ENSP00000360730.3; ENSG00000131724.11. [P78552-1]
DR GeneID; 3597; -.
DR KEGG; hsa:3597; -.
DR MANE-Select; ENST00000371666.8; ENSP00000360730.3; NM_001560.3; NP_001551.1.
DR UCSC; uc004eqr.2; human. [P78552-1]
DR CTD; 3597; -.
DR DisGeNET; 3597; -.
DR GeneCards; IL13RA1; -.
DR HGNC; HGNC:5974; IL13RA1.
DR HPA; ENSG00000131724; Low tissue specificity.
DR MIM; 300119; gene.
DR neXtProt; NX_P78552; -.
DR OpenTargets; ENSG00000131724; -.
DR PharmGKB; PA200; -.
DR VEuPathDB; HostDB:ENSG00000131724; -.
DR eggNOG; ENOG502RYXH; Eukaryota.
DR GeneTree; ENSGT00940000160896; -.
DR HOGENOM; CLU_039945_1_0_1; -.
DR InParanoid; P78552; -.
DR OMA; YDICEKQ; -.
DR OrthoDB; 1151666at2759; -.
DR PhylomeDB; P78552; -.
DR TreeFam; TF331549; -.
DR PathwayCommons; P78552; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P78552; -.
DR SIGNOR; P78552; -.
DR BioGRID-ORCS; 3597; 8 hits in 706 CRISPR screens.
DR ChiTaRS; IL13RA1; human.
DR EvolutionaryTrace; P78552; -.
DR GeneWiki; Interleukin_13_receptor,_alpha_1; -.
DR GenomeRNAi; 3597; -.
DR Pharos; P78552; Tbio.
DR PRO; PR:P78552; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P78552; protein.
DR Bgee; ENSG00000131724; Expressed in esophagus squamous epithelium and 201 other tissues.
DR ExpressionAtlas; P78552; baseline and differential.
DR Genevisible; P78552; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005898; C:interleukin-13 receptor complex; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; 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:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:GOC.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
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; IPR040566; Il13Ra_Ig.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF18001; Il13Ra_Ig; 1.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..427
FT /note="Interleukin-13 receptor subunit alpha-1"
FT /id="PRO_0000010939"
FT TOPO_DOM 22..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..123
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 128..226
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 227..339
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 327..331
FT /note="WSXWS motif"
FT MOTIF 374..382
FT /note="Box 1 motif"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
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 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..102
FT /evidence="ECO:0000269|PubMed:18243101"
FT DISULFID 95..117
FT /evidence="ECO:0000269|PubMed:18243101"
FT DISULFID 134..144
FT /evidence="ECO:0000269|PubMed:18243101"
FT DISULFID 173..185
FT /evidence="ECO:0000269|PubMed:18243101"
FT DISULFID 257..320
FT /evidence="ECO:0000269|PubMed:18243101"
FT DISULFID 282..296
FT /evidence="ECO:0000269|PubMed:18243101"
FT VAR_SEQ 278..279
FT /note="QE -> RF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_055587"
FT VAR_SEQ 280..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_055588"
FT CONFLICT 130
FT /note="T -> I (in Ref. 3; AAB37127)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="G -> D (in Ref. 3; AAB37127)"
FT /evidence="ECO:0000305"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:3BPO"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3BPO"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5E4E"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5E4E"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3BPO"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3BPN"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:3BPO"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5E4E"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4HWB"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:4HWB"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4HWB"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:3BPO"
SQ SEQUENCE 427 AA; 48760 MW; 5983B3E8F554107B CRC64;
MEWPARLCGL WALLLCAGGG GGGGGAAPTE TQPPVTNLSV SVENLCTVIW TWNPPEGASS
NCSLWYFSHF GDKQDKKIAP ETRRSIEVPL NERICLQVGS QCSTNESEKP SILVEKCISP
PEGDPESAVT ELQCIWHNLS YMKCSWLPGR NTSPDTNYTL YYWHRSLEKI HQCENIFREG
QYFGCSFDLT KVKDSSFEQH SVQIMVKDNA GKIKPSFNIV PLTSRVKPDP PHIKNLSFHN
DDLYVQWENP QNFISRCLFY EVEVNNSQTE THNVFYVQEA KCENPEFERN VENTSCFMVP
GVLPDTLNTV RIRVKTNKLC YEDDKLWSNW SQEMSIGKKR NSTLYITMLL IVPVIVAGAI
IVLLLYLKRL KIIIFPPIPD PGKIFKEMFG DQNDDTLHWK KYDIYEKQTK EETDSVVLIE
NLKKASQ
