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I20RA_HUMAN
ID   I20RA_HUMAN             Reviewed;         553 AA.
AC   Q9UHF4; B4DLR5; F5H675; Q14CW2; Q6UWA9; Q96SH8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Interleukin-20 receptor subunit alpha;
DE            Short=IL-20 receptor subunit alpha;
DE            Short=IL-20R-alpha;
DE            Short=IL-20RA;
DE   AltName: Full=Cytokine receptor class-II member 8;
DE   AltName: Full=Cytokine receptor family 2 member 8;
DE            Short=CRF2-8;
DE   AltName: Full=IL-20R1;
DE   AltName: Full=ZcytoR7;
DE   Flags: Precursor;
GN   Name=IL20RA; ORFNames=UNQ681/PRO1315;
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), AND VARIANTS ILE-259 AND PHE-382.
RA   Lok S., Kho C.-J., Jelmberg A., Adams R., Whitmore T., Farrah T.,
RA   O'Hara P.;
RT   "Homo sapiens cytokine receptor homolog.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-259.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ILE-259.
RC   TISSUE=Fibroblast;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-259.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-259.
RC   TISSUE=Brain;
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   [7]
RP   PROTEIN SEQUENCE OF 30-44.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [8]
RP   SUBUNIT, LIGAND-BINDING, AND TISSUE SPECIFICITY.
RX   PubMed=11163236; DOI=10.1016/s0092-8674(01)00187-8;
RA   Blumberg H., Conklin D., Xu W.F., Grossmann A., Brender T., Carollo S.,
RA   Eagan M., Foster D., Haldeman B.A., Hammond A., Haugen H., Jelinek L.,
RA   Kelly J.D., Madden K., Maurer M.F., Parrish-Novak J., Prunkard D.,
RA   Sexson S., Sprecher C., Waggie K., West J., Whitmore T.E., Yao L.,
RA   Kuechle M.K., Dale B.A., Chandrasekher Y.A.;
RT   "Interleukin 20: discovery, receptor identification, and role in epidermal
RT   function.";
RL   Cell 104:9-19(2001).
RN   [9]
RP   LIGAND-BINDING.
RX   PubMed=11564763; DOI=10.4049/jimmunol.167.7.3545;
RA   Dumoutier L., Leemans C., Lejeune D., Kotenko S.V., Renauld J.-C.;
RT   "STAT activation by IL-19, IL-20 and mda-7 through IL-20 receptor complexes
RT   of two types.";
RL   J. Immunol. 167:3545-3549(2001).
RN   [10]
RP   SUBUNIT, AND LIGAND-BINDING.
RX   PubMed=12351624; DOI=10.1074/jbc.m205114200;
RA   Parrish-Novak J., Xu W., Brender T., Yao L., Jones C., West J., Brandt C.,
RA   Jelinek L., Madden K., McKernan P.A., Foster D.C., Jaspers S.,
RA   Chandrasekher Y.A.;
RT   "Interleukins 19, 20, and 24 signal through two distinct receptor
RT   complexes. Differences in receptor-ligand interactions mediate unique
RT   biological functions.";
RL   J. Biol. Chem. 277:47517-47523(2002).
RN   [11]
RP   SUBUNIT, AND LIGAND-BINDING.
RX   PubMed=14580208; DOI=10.1021/bi0354583;
RA   Pletnev S., Magracheva E., Kozlov S., Tobin G., Kotenko S.V., Wlodawer A.,
RA   Zdanov A.;
RT   "Characterization of the recombinant extracellular domains of human
RT   interleukin-20 receptors and their complexes with interleukin-19 and
RT   interleukin-20.";
RL   Biochemistry 42:12617-12624(2003).
RN   [12]
RP   SUBUNIT, LIGAND-BINDING, AND TISSUE SPECIFICITY.
RX   PubMed=14764663; DOI=10.4049/jimmunol.172.4.2006;
RA   Sheikh F., Baurin V.V., Lewis-Antes A., Shah N.K., Smirnov S.V.,
RA   Anantha S., Dickensheets H., Dumoutier L., Renauld J.-C., Zdanov A.,
RA   Donnelly R.P., Kotenko S.V.;
RT   "IL-26 signals through a novel receptor complex composed of IL-20 receptor
RT   1 and IL-10 receptor 2.";
RL   J. Immunol. 172:2006-2010(2004).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-245 IN COMPLEX WITH IL20RB AND
RP   IL20, SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=22802649; DOI=10.1073/pnas.1117551109;
RA   Logsdon N.J., Deshpande A., Harris B.D., Rajashankar K.R., Walter M.R.;
RT   "Structural basis for receptor sharing and activation by interleukin-20
RT   receptor-2 (IL-20R2) binding cytokines.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12704-12709(2012).
CC   -!- FUNCTION: The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and
CC       IL24. The IL20RA/IL10RB dimer is a receptor for IL26.
CC   -!- SUBUNIT: Heterodimer with IL20RB and heterodimer with IL10RB.
CC       {ECO:0000269|PubMed:11163236, ECO:0000269|PubMed:12351624,
CC       ECO:0000269|PubMed:14580208, ECO:0000269|PubMed:14764663,
CC       ECO:0000269|PubMed:22802649}.
CC   -!- INTERACTION:
CC       Q9UHF4; PRO_0000015381 [Q9NYY1]: IL20; NbExp=4; IntAct=EBI-2933034, EBI-14022785;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UHF4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UHF4-2; Sequence=VSP_011497, VSP_011498;
CC       Name=3;
CC         IsoId=Q9UHF4-3; Sequence=VSP_054741;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skin and
CC       testis and high levels in brain. Highly expressed in psoriatic skin.
CC       {ECO:0000269|PubMed:11163236, ECO:0000269|PubMed:14764663}.
CC   -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC       {ECO:0000305}.
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DR   EMBL; AF184971; AAF01320.1; -; mRNA.
DR   EMBL; AY358883; AAQ89242.1; -; mRNA.
DR   EMBL; AK297121; BAG59627.1; -; mRNA.
DR   EMBL; AL135902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47936.1; -; Genomic_DNA.
DR   EMBL; BC113574; AAI13575.1; -; mRNA.
DR   EMBL; BC113602; AAI13603.1; -; mRNA.
DR   CCDS; CCDS5181.1; -. [Q9UHF4-1]
DR   CCDS; CCDS64535.1; -. [Q9UHF4-2]
DR   CCDS; CCDS64536.1; -. [Q9UHF4-3]
DR   RefSeq; NP_001265651.1; NM_001278722.1. [Q9UHF4-3]
DR   RefSeq; NP_001265652.1; NM_001278723.1. [Q9UHF4-2]
DR   RefSeq; NP_001265653.1; NM_001278724.1.
DR   RefSeq; NP_055247.3; NM_014432.3. [Q9UHF4-1]
DR   RefSeq; XP_011534206.1; XM_011535904.2. [Q9UHF4-2]
DR   PDB; 4DOH; X-ray; 2.80 A; E/R=29-245.
DR   PDBsum; 4DOH; -.
DR   AlphaFoldDB; Q9UHF4; -.
DR   SMR; Q9UHF4; -.
DR   BioGRID; 119804; 33.
DR   IntAct; Q9UHF4; 34.
DR   STRING; 9606.ENSP00000314976; -.
DR   GlyGen; Q9UHF4; 6 sites.
DR   BioMuta; IL20RA; -.
DR   DMDM; 145559483; -.
DR   PaxDb; Q9UHF4; -.
DR   PeptideAtlas; Q9UHF4; -.
DR   PRIDE; Q9UHF4; -.
DR   ProteomicsDB; 27103; -.
DR   ProteomicsDB; 84341; -. [Q9UHF4-1]
DR   ProteomicsDB; 84342; -. [Q9UHF4-2]
DR   Antibodypedia; 33022; 385 antibodies from 30 providers.
DR   DNASU; 53832; -.
DR   Ensembl; ENST00000316649.10; ENSP00000314976.5; ENSG00000016402.14. [Q9UHF4-1]
DR   Ensembl; ENST00000367748.4; ENSP00000356722.1; ENSG00000016402.14. [Q9UHF4-2]
DR   Ensembl; ENST00000541547.5; ENSP00000437843.1; ENSG00000016402.14. [Q9UHF4-3]
DR   GeneID; 53832; -.
DR   KEGG; hsa:53832; -.
DR   MANE-Select; ENST00000316649.10; ENSP00000314976.5; NM_014432.4; NP_055247.4.
DR   UCSC; uc003qhj.5; human. [Q9UHF4-1]
DR   CTD; 53832; -.
DR   DisGeNET; 53832; -.
DR   GeneCards; IL20RA; -.
DR   HGNC; HGNC:6003; IL20RA.
DR   HPA; ENSG00000016402; Tissue enhanced (breast, skin).
DR   MIM; 605620; gene.
DR   neXtProt; NX_Q9UHF4; -.
DR   OpenTargets; ENSG00000016402; -.
DR   PharmGKB; PA29818; -.
DR   VEuPathDB; HostDB:ENSG00000016402; -.
DR   eggNOG; ENOG502RPFC; Eukaryota.
DR   GeneTree; ENSGT00940000157314; -.
DR   HOGENOM; CLU_527430_0_0_1; -.
DR   InParanoid; Q9UHF4; -.
DR   OMA; MINFITL; -.
DR   OrthoDB; 1078220at2759; -.
DR   PhylomeDB; Q9UHF4; -.
DR   TreeFam; TF334107; -.
DR   PathwayCommons; Q9UHF4; -.
DR   Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR   SignaLink; Q9UHF4; -.
DR   SIGNOR; Q9UHF4; -.
DR   BioGRID-ORCS; 53832; 6 hits in 1068 CRISPR screens.
DR   ChiTaRS; IL20RA; human.
DR   GeneWiki; Interleukin_20_receptor,_alpha_subunit; -.
DR   GenomeRNAi; 53832; -.
DR   Pharos; Q9UHF4; Tbio.
DR   PRO; PR:Q9UHF4; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9UHF4; protein.
DR   Bgee; ENSG00000016402; Expressed in olfactory segment of nasal mucosa and 132 other tissues.
DR   ExpressionAtlas; Q9UHF4; baseline and differential.
DR   Genevisible; Q9UHF4; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0042015; F:interleukin-20 binding; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0045124; P:regulation of bone resorption; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015713; IL-20_rcpt_alpha.
DR   InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR   PANTHER; PTHR20859:SF21; PTHR20859:SF21; 1.
DR   Pfam; PF09294; Interfer-bind; 1.
DR   Pfam; PF01108; Tissue_fac; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           30..553
FT                   /note="Interleukin-20 receptor subunit alpha"
FT                   /id="PRO_0000011036"
FT   TOPO_DOM        30..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..553
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..135
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          136..242
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          333..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..95
FT                   /evidence="ECO:0000269|PubMed:22802649"
FT   DISULFID        215..236
FT                   /evidence="ECO:0000269|PubMed:22802649"
FT   VAR_SEQ         1..111
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_011497"
FT   VAR_SEQ         1..49
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054741"
FT   VAR_SEQ         112..135
FT                   /note="VKAIWGTKCSKWAESGRFYPFLET -> MSYNGLHQRVFKELKLLTLCSISS
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_011498"
FT   VARIANT         259
FT                   /note="V -> I (in dbSNP:rs1555498)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.1, ECO:0000269|Ref.5"
FT                   /id="VAR_031613"
FT   VARIANT         382
FT                   /note="L -> F (in dbSNP:rs1342642)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_031614"
FT   CONFLICT        96
FT                   /note="D -> V (in Ref. 3; BAG59627)"
FT                   /evidence="ECO:0000305"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          68..75
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          88..96
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          108..118
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   HELIX           131..134
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          180..187
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   TURN            188..191
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          192..198
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          213..221
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:4DOH"
FT   STRAND          233..238
FT                   /evidence="ECO:0007829|PDB:4DOH"
SQ   SEQUENCE   553 AA;  62485 MW;  D5C2621FDC848328 CRC64;
     MRAPGRPALR PLPLPPLLLL LLAAPWGRAV PCVSGGLPKP ANITFLSINM KNVLQWTPPE
     GLQGVKVTYT VQYFIYGQKK WLNKSECRNI NRTYCDLSAE TSDYEHQYYA KVKAIWGTKC
     SKWAESGRFY PFLETQIGPP EVALTTDEKS ISVVLTAPEK WKRNPEDLPV SMQQIYSNLK
     YNVSVLNTKS NRTWSQCVTN HTLVLTWLEP NTLYCVHVES FVPGPPRRAQ PSEKQCARTL
     KDQSSEFKAK IIFWYVLPVS ITVFLFSVMG YSIYRYIHVG KEKHPANLIL IYGNEFDKRF
     FVPAEKIVIN FITLNISDDS KISHQDMSLL GKSSDVSSLN DPQPSGNLRP PQEEEEVKHL
     GYASHLMEIF CDSEENTEGT SLTQQESLSR TIPPDKTVIE YEYDVRTTDI CAGPEEQELS
     LQEEVSTQGT LLESQAALAV LGPQTLQYSY TPQLQDLDPL AQEHTDSEEG PEEEPSTTLV
     DWDPQTGRLC IPSLSSFDQD SEGCEPSEGD GLGEEGLLSR LYEEPAPDRP PGENETYLMQ
     FMEEWGLYVQ MEN
 
 
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