XIRP2_HUMAN
ID XIRP2_HUMAN Reviewed; 3374 AA.
AC A4UGR9; A0PJ94; B2BBS0; B2BBS1; B2BBS4; B3KVH0; J3KNB1; Q53R52; Q5MJ67;
AC Q702N7; Q86T36; Q86T38; Q86T46; Q86T51; Q86T53; Q86T55; Q86T79; Q86TB6;
AC Q8N1M9; Q8N3R5; Q8TBV6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Xin actin-binding repeat-containing protein 2;
DE AltName: Full=Beta-xin;
DE AltName: Full=Cardiomyopathy-associated protein 3;
DE AltName: Full=Xeplin;
GN Name=XIRP2; Synonyms=CMYA3;
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 3).
RA Luo J., Liu M., Wu X.;
RT "A novel gene containing a Xin repeat.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 6 AND 7).
RC TISSUE=Heart, and Testis;
RA Wang K., Xie L., Tsai W.L., Gutierrez-Cruz G.;
RT "bXin: genes, splice variants and cellular distribution of a family of
RT proteins implicated.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 901-1683 (ISOFORMS 1/2/3).
RC TISSUE=Tongue;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-748 (ISOFORMS 1/2/3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3177-3374 (ISOFORMS 1/2).
RC TISSUE=Skeletal muscle;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 361-1380 (ISOFORMS 1/2/3), FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH F-ACTIN.
RC TISSUE=Skeletal muscle;
RX PubMed=15454575; DOI=10.1242/jcs.01406;
RA Pacholsky D., Vakeel P., Himmel M., Loewe T., Stradal T., Rottner K.,
RA Fuerst D.O., van der Ven P.F.M.;
RT "Xin repeats define a novel actin-binding motif.";
RL J. Cell Sci. 117:5257-5268(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-3374 (ISOFORMS 1/2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP VARIANT VAL-2769.
RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT "Homozygous missense mutation in the LMAN2L gene segregates with
RT intellectual disability in a large consanguineous Pakistani family.";
RL J. Med. Genet. 53:138-144(2016).
CC -!- FUNCTION: Protects actin filaments from depolymerization.
CC {ECO:0000269|PubMed:15454575}.
CC -!- SUBUNIT: Interacts with ACTN2 (By similarity). Interacts with F-actin.
CC {ECO:0000250, ECO:0000269|PubMed:15454575}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15454575}.
CC Note=Colocalizes with actin stress fibers. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=A4UGR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4UGR9-2; Sequence=VSP_030846;
CC Name=3;
CC IsoId=A4UGR9-3; Sequence=VSP_030847, VSP_030848;
CC Name=4;
CC IsoId=A4UGR9-4; Sequence=VSP_035717, VSP_035719, VSP_035720;
CC Name=5;
CC IsoId=A4UGR9-5; Sequence=VSP_035719, VSP_035720;
CC Name=6;
CC IsoId=A4UGR9-6; Sequence=VSP_035717, VSP_035718, VSP_035719,
CC VSP_035720;
CC Name=7;
CC IsoId=A4UGR9-7; Sequence=VSP_030846, VSP_035719, VSP_035720;
CC Name=8;
CC IsoId=A4UGR9-8; Sequence=VSP_035717;
CC -!- DOMAIN: Xin repeats bind F-actin.
CC -!- MISCELLANEOUS: 'Xin' means 'heart' in Chinese.
CC -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00721}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18673.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAY24138.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38624.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAD89958.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=CAD91141.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AY820969; AAV87913.1; -; mRNA.
DR EMBL; EF119717; ABO69245.1; -; mRNA.
DR EMBL; EF119718; ABO69246.1; -; mRNA.
DR EMBL; EF119719; ABO69247.1; -; mRNA.
DR EMBL; EF119720; ABO69248.1; -; mRNA.
DR EMBL; EF119721; ABO69249.1; -; mRNA.
DR EMBL; EF119722; ABO69250.1; -; mRNA.
DR EMBL; EF119711; ABO69251.1; -; mRNA.
DR EMBL; AK096430; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK122889; BAG53782.1; -; mRNA.
DR EMBL; AC093684; AAY24138.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC108494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11311.1; -; Genomic_DNA.
DR EMBL; BC018673; AAH18673.1; ALT_SEQ; mRNA.
DR EMBL; BC022888; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ626901; CAF25193.1; -; mRNA.
DR EMBL; AL832331; CAD38624.1; ALT_SEQ; mRNA.
DR EMBL; AL831970; CAD89919.1; -; mRNA.
DR EMBL; AL832452; CAD89958.1; ALT_SEQ; mRNA.
DR EMBL; AL832336; CAD91137.1; -; mRNA.
DR EMBL; AL831985; CAD91139.1; -; mRNA.
DR EMBL; AL833291; CAD91141.2; ALT_SEQ; mRNA.
DR EMBL; AL832011; CAD91146.1; -; mRNA.
DR EMBL; AL832360; CAD91154.1; -; mRNA.
DR EMBL; AL832382; CAD91156.1; -; mRNA.
DR CCDS; CCDS42768.1; -. [A4UGR9-4]
DR CCDS; CCDS42769.1; -. [A4UGR9-8]
DR CCDS; CCDS56143.1; -. [A4UGR9-6]
DR CCDS; CCDS56144.1; -. [A4UGR9-2]
DR CCDS; CCDS56145.1; -. [A4UGR9-7]
DR RefSeq; NP_001073278.1; NM_001079810.3. [A4UGR9-4]
DR RefSeq; NP_001186072.1; NM_001199143.1. [A4UGR9-6]
DR RefSeq; NP_001186073.1; NM_001199144.1. [A4UGR9-2]
DR RefSeq; NP_001186074.1; NM_001199145.1. [A4UGR9-7]
DR RefSeq; NP_689594.4; NM_152381.5. [A4UGR9-8]
DR PDB; 4F14; X-ray; 1.20 A; B=2245-2257.
DR PDBsum; 4F14; -.
DR SMR; A4UGR9; -.
DR BioGRID; 126192; 22.
DR IntAct; A4UGR9; 10.
DR STRING; 9606.ENSP00000386840; -.
DR GlyGen; A4UGR9; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; A4UGR9; -.
DR PhosphoSitePlus; A4UGR9; -.
DR BioMuta; XIRP2; -.
DR EPD; A4UGR9; -.
DR jPOST; A4UGR9; -.
DR MassIVE; A4UGR9; -.
DR PaxDb; A4UGR9; -.
DR PeptideAtlas; A4UGR9; -.
DR PRIDE; A4UGR9; -.
DR ProteomicsDB; 697; -. [A4UGR9-1]
DR ProteomicsDB; 698; -. [A4UGR9-2]
DR ProteomicsDB; 699; -. [A4UGR9-3]
DR ProteomicsDB; 700; -. [A4UGR9-4]
DR ProteomicsDB; 701; -. [A4UGR9-5]
DR ProteomicsDB; 702; -. [A4UGR9-6]
DR ProteomicsDB; 703; -. [A4UGR9-7]
DR Antibodypedia; 33785; 55 antibodies from 15 providers.
DR DNASU; 129446; -.
DR Ensembl; ENST00000409043.5; ENSP00000386454.1; ENSG00000163092.22. [A4UGR9-4]
DR Ensembl; ENST00000409195.6; ENSP00000386840.2; ENSG00000163092.22. [A4UGR9-8]
DR Ensembl; ENST00000409273.6; ENSP00000387255.1; ENSG00000163092.22. [A4UGR9-2]
DR Ensembl; ENST00000409605.1; ENSP00000386981.1; ENSG00000163092.22. [A4UGR9-7]
DR Ensembl; ENST00000409728.5; ENSP00000386619.1; ENSG00000163092.22. [A4UGR9-6]
DR Ensembl; ENST00000628543.2; ENSP00000486198.1; ENSG00000163092.22. [A4UGR9-1]
DR GeneID; 129446; -.
DR KEGG; hsa:129446; -.
DR MANE-Select; ENST00000409195.6; ENSP00000386840.2; NM_152381.6; NP_689594.4. [A4UGR9-8]
DR UCSC; uc002udx.4; human. [A4UGR9-1]
DR CTD; 129446; -.
DR DisGeNET; 129446; -.
DR GeneCards; XIRP2; -.
DR HGNC; HGNC:14303; XIRP2.
DR HPA; ENSG00000163092; Group enriched (skeletal muscle, tongue).
DR MIM; 609778; gene.
DR neXtProt; NX_A4UGR9; -.
DR OpenTargets; ENSG00000163092; -.
DR PharmGKB; PA162409337; -.
DR VEuPathDB; HostDB:ENSG00000163092; -.
DR eggNOG; ENOG502SF50; Eukaryota.
DR GeneTree; ENSGT00530000063779; -.
DR HOGENOM; CLU_013855_0_0_1; -.
DR InParanoid; A4UGR9; -.
DR OrthoDB; 30028at2759; -.
DR PhylomeDB; A4UGR9; -.
DR TreeFam; TF330745; -.
DR PathwayCommons; A4UGR9; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; A4UGR9; -.
DR BioGRID-ORCS; 129446; 5 hits in 1064 CRISPR screens.
DR ChiTaRS; XIRP2; human.
DR GeneWiki; XIRP2; -.
DR GenomeRNAi; 129446; -.
DR Pharos; A4UGR9; Tbio.
DR PRO; PR:A4UGR9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; A4UGR9; protein.
DR Bgee; ENSG00000163092; Expressed in deltoid and 95 other tissues.
DR ExpressionAtlas; A4UGR9; baseline and differential.
DR Genevisible; A4UGR9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR GO; GO:0045216; P:cell-cell junction organization; IEA:Ensembl.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR InterPro; IPR012510; Actin-binding_Xin_repeat.
DR InterPro; IPR030072; XIRP1/XIRP2.
DR InterPro; IPR030107; XIRP2.
DR PANTHER; PTHR22591; PTHR22591; 1.
DR PANTHER; PTHR22591:SF1; PTHR22591:SF1; 1.
DR Pfam; PF08043; Xin; 20.
DR PROSITE; PS51389; XIN; 28.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW Coiled coil; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..3374
FT /note="Xin actin-binding repeat-containing protein 2"
FT /id="PRO_0000316987"
FT REPEAT 362..377
FT /note="Xin 1"
FT REPEAT 397..412
FT /note="Xin 2"
FT REPEAT 437..452
FT /note="Xin 3"
FT REPEAT 474..489
FT /note="Xin 4"
FT REPEAT 512..527
FT /note="Xin 5"
FT REPEAT 552..567
FT /note="Xin 6"
FT REPEAT 590..605
FT /note="Xin 7"
FT REPEAT 628..643
FT /note="Xin 8"
FT REPEAT 661..676
FT /note="Xin 9"
FT REPEAT 695..710
FT /note="Xin 10"
FT REPEAT 732..747
FT /note="Xin 11"
FT REPEAT 768..783
FT /note="Xin 12"
FT REPEAT 799..814
FT /note="Xin 13"
FT REPEAT 837..852
FT /note="Xin 14"
FT REPEAT 875..890
FT /note="Xin 15"
FT REPEAT 914..929
FT /note="Xin 16"
FT REPEAT 947..962
FT /note="Xin 17"
FT REPEAT 985..1000
FT /note="Xin 18"
FT REPEAT 1020..1035
FT /note="Xin 19"
FT REPEAT 1059..1074
FT /note="Xin 20"
FT REPEAT 1095..1110
FT /note="Xin 21"
FT REPEAT 1132..1147
FT /note="Xin 22"
FT REPEAT 1170..1185
FT /note="Xin 23"
FT REPEAT 1207..1222
FT /note="Xin 24"
FT REPEAT 1241..1256
FT /note="Xin 25"
FT REPEAT 1272..1287
FT /note="Xin 26"
FT REPEAT 1310..1325
FT /note="Xin 27"
FT REPEAT 1345..1360
FT /note="Xin 28"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2098..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2601..2656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2860..3007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3353..3374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1736..1763
FT /evidence="ECO:0000255"
FT COILED 2369..2394
FT /evidence="ECO:0000255"
FT COILED 2768..2792
FT /evidence="ECO:0000255"
FT COILED 2823..2849
FT /evidence="ECO:0000255"
FT COMPBIAS 102..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2212..2238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2616..2643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2860..2890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2891..2929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2944..2971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2989..3003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4U4S6"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 1629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 1989
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 1994
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 2222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4U4S6"
FT MOD_RES 2276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 2318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 3059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4U4S6"
FT MOD_RES 3297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_030846"
FT VAR_SEQ 1
FT /note="M -> MFPMQKGSLNLLRQKWESCDYQRSECHPRDSHCTIFQPQESKLLAPE
FT GEVVSAPQSLDPTSLPYSTGEEMWSSKPEEKDSVDKSNNTREYGRPEVLKEDSLSSRRR
FT IERFSIALDELRSVFEAPKSGNKPAEYGGKEVEIERSLCSPAFKSHPGSQLEDSVKDSD
FT KKGKETSFDKM (in isoform 4, isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_035717"
FT VAR_SEQ 13
FT /note="A -> AVFSTDQAQILRLHLHPKLTKTPKNSLKSSTYIS (in isoform
FT 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_035718"
FT VAR_SEQ 218..771
FT /note="TESEYEETFKPSSVVSTSSTSCVSTSQRKETSTTRYSDHSVTSSTLAQINAT
FT SSGMTEEFPPPPPDVLQTSVDVTAFSQSPELPSPPRRLPVPKDVYSKQRNLYELNRLYK
FT HIHPELRKNLEKDYISEVSEIVSSQMNSGSSVSADVQQARYVFENTNDSSQKDLNSERE
FT YLEWDEILKGEVQSIRWIFENQPLDSINNGSPDEGDISRGIADQEIIAGGDVKYTTWMF
FT ETQPIDTLGAYSSDTVENAEKIPELARGDVCTARWMFETRPLDSMNKMHQSQEESAVTI
FT SKDITGGDVKTVRYMFETQHLDQLGQLHSVDEVHLLQLRSELKEIKGNVKRSIKCFETQ
FT PLYVIRDGSGQMLEIKTVHREDVEKGDVRTARWMFETQPLDTINKDITEIKVVRGISME
FT ENVKGGVSKAKWLFETQPLEKIKESEEVIIEKEKIIGTDVSRKCWMFETQPLDILKEVP
FT DADSLQREEIIGGDVQTTKHLFETLPIEALKDSPDIGKLQKITASEEEKGDVRHQKWIF
FT ETQPLEDIRKDKKEYTRTVKLEEVDRGDVK -> KLLLQDKEICILCQKTVYPMECLVA
FT DKQNFHKSCFRCHHCNSKLSLGNYASLHGQIYCKPHFKQLFKSKGNYDEGFGHKQHKDR
FT WNCKNQSRSVDFIPNEEPNMCKNIAENTLVPGDRNEHLDAGNSEGQRNDLRKLGERGKL
FT KVIWPPSKEIPKKTLPFEEELKMSKPKWPPEMTTLLSPEFKSESLLEDVRTPENKGQRQ
FT DHFPFLQPYLQSTHVCQKEDVIGIKEMKMPEGRKDEKKEGRKNVQDRPSEAEDTKSNRK
FT SAMDLNDNNNVIVQSAEKEKNEKTNQTNGAEVLQVTNTDDEMMPENHKENLNKNNNNNY
FT VAVSYLNNCRQKTSILEFLDLLPLSSEANDTANEYEIEKLENTSRISELLGIFESEKTY
FT SRNVLAMALKKQTDRAAAGSPVQPAPKPSLSRGLMVKGGSSIISPDTNLLNIKGSHSKS
FT KNLHFFFSNTVKITAFSKKNENIFNCDLIDSVDQIKNMPCLDLREFGKDVKPWHVETTE
FT AARNNENTGFDALSHECTAKPLFPRVEVQSEQLTVEEQIKRNRCYSDTE (in
FT isoform 4, isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_035719"
FT VAR_SEQ 772..3374
FT /note="Missing (in isoform 4, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_035720"
FT VAR_SEQ 3344..3345
FT /note="EA -> GK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030847"
FT VAR_SEQ 3346..3374
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030848"
FT VARIANT 450
FT /note="P -> A (in dbSNP:rs16853305)"
FT /id="VAR_038449"
FT VARIANT 457
FT /note="Y -> H (in dbSNP:rs16853306)"
FT /id="VAR_038450"
FT VARIANT 1397
FT /note="I -> T (in dbSNP:rs7588159)"
FT /id="VAR_038451"
FT VARIANT 1488
FT /note="I -> T (in dbSNP:rs7591107)"
FT /id="VAR_038452"
FT VARIANT 1626
FT /note="R -> H (in dbSNP:rs16853309)"
FT /id="VAR_038453"
FT VARIANT 1833
FT /note="N -> S (in dbSNP:rs7607246)"
FT /id="VAR_038454"
FT VARIANT 2423
FT /note="L -> R (in dbSNP:rs16853326)"
FT /id="VAR_038455"
FT VARIANT 2553
FT /note="S -> N (in dbSNP:rs16853328)"
FT /id="VAR_038456"
FT VARIANT 2595
FT /note="H -> Y (in dbSNP:rs16853329)"
FT /id="VAR_038457"
FT VARIANT 2607
FT /note="V -> I (in dbSNP:rs16853330)"
FT /id="VAR_038458"
FT VARIANT 2728
FT /note="G -> D (in dbSNP:rs3749002)"
FT /id="VAR_038459"
FT VARIANT 2769
FT /note="I -> V (in dbSNP:rs781323589)"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076434"
FT VARIANT 2910
FT /note="A -> T (in dbSNP:rs16853331)"
FT /id="VAR_038460"
FT VARIANT 2975
FT /note="Y -> C (in dbSNP:rs3749003)"
FT /id="VAR_038461"
FT VARIANT 3022
FT /note="I -> V (in dbSNP:rs3749004)"
FT /id="VAR_038462"
FT VARIANT 3202
FT /note="G -> E (in dbSNP:rs16853333)"
FT /id="VAR_038463"
FT CONFLICT 112
FT /note="E -> G (in Ref. 6; AAH18673)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="Q -> L (in Ref. 7; CAF25193 and 8; CAD38624)"
FT /evidence="ECO:0000305"
FT CONFLICT 1144
FT /note="Q -> R (in Ref. 7; CAF25193 and 8; CAD38624)"
FT /evidence="ECO:0000305"
FT CONFLICT 2318
FT /note="S -> P (in Ref. 8; CAD91137)"
FT /evidence="ECO:0000305"
FT CONFLICT 2522
FT /note="H -> P (in Ref. 8; CAD91146)"
FT /evidence="ECO:0000305"
FT CONFLICT 2661
FT /note="I -> M (in Ref. 8; CAD91139)"
FT /evidence="ECO:0000305"
FT CONFLICT 2665
FT /note="K -> N (in Ref. 8; CAD89958)"
FT /evidence="ECO:0000305"
FT CONFLICT 2713
FT /note="Q -> R (in Ref. 8; CAD89919)"
FT /evidence="ECO:0000305"
FT CONFLICT 2967
FT /note="S -> A (in Ref. 8; CAD91141)"
FT /evidence="ECO:0000305"
FT CONFLICT 2996
FT /note="S -> P (in Ref. 8; CAD89919)"
FT /evidence="ECO:0000305"
FT CONFLICT 3013
FT /note="T -> A (in Ref. 8; CAD91154)"
FT /evidence="ECO:0000305"
FT CONFLICT 3079
FT /note="E -> G (in Ref. 8; CAD91137)"
FT /evidence="ECO:0000305"
FT CONFLICT 3121
FT /note="I -> T (in Ref. 8; CAD89958)"
FT /evidence="ECO:0000305"
FT CONFLICT 3166
FT /note="E -> G (in Ref. 8; CAD91141)"
FT /evidence="ECO:0000305"
FT CONFLICT 3259
FT /note="M -> V (in Ref. 8; CAD91139)"
FT /evidence="ECO:0000305"
FT CONFLICT 3264
FT /note="S -> L (in Ref. 8; CAD91141)"
FT /evidence="ECO:0000305"
FT CONFLICT 3329
FT /note="T -> A (in Ref. 8; CAD91146)"
FT /evidence="ECO:0000305"
FT VARIANT A4UGR9-4:757
FT /note="R -> G (in dbSNP:rs3749005)"
FT /evidence="ECO:0000305"
FT /id="VAR_082888"
FT VARIANT A4UGR9-4:885
FT /note="V -> G (in dbSNP:rs3749006)"
FT /evidence="ECO:0000305"
FT /id="VAR_082889"
FT VARIANT A4UGR9-4:905
FT /note="E -> Q (in dbSNP:rs16853344)"
FT /evidence="ECO:0000305"
FT /id="VAR_082890"
SQ SEQUENCE 3374 AA; 382300 MW; F02A01BD2D621F45 CRC64;
MSPESGHSRI FEATAGPNKP ESGFAEDSAA RGEGVSDLHE VVSLKERMAR YQAAVSRGDC
RSFSANMMEE SEMCAVPGGL AKVKKQFEDE ITSSRNTFAQ YQYQHQNRSE QEAIHSSQVG
TSRSSQEMAR NEQEGSKVQK IDVHGTEMVS HLEKHTEEVN QASQFHQYVQ ETVIDTPEDE
EIPKVSTKLL KEQFEKSAQE KILYSDKEMT TPAKQIKTES EYEETFKPSS VVSTSSTSCV
STSQRKETST TRYSDHSVTS STLAQINATS SGMTEEFPPP PPDVLQTSVD VTAFSQSPEL
PSPPRRLPVP KDVYSKQRNL YELNRLYKHI HPELRKNLEK DYISEVSEIV SSQMNSGSSV
SADVQQARYV FENTNDSSQK DLNSEREYLE WDEILKGEVQ SIRWIFENQP LDSINNGSPD
EGDISRGIAD QEIIAGGDVK YTTWMFETQP IDTLGAYSSD TVENAEKIPE LARGDVCTAR
WMFETRPLDS MNKMHQSQEE SAVTISKDIT GGDVKTVRYM FETQHLDQLG QLHSVDEVHL
LQLRSELKEI KGNVKRSIKC FETQPLYVIR DGSGQMLEIK TVHREDVEKG DVRTARWMFE
TQPLDTINKD ITEIKVVRGI SMEENVKGGV SKAKWLFETQ PLEKIKESEE VIIEKEKIIG
TDVSRKCWMF ETQPLDILKE VPDADSLQRE EIIGGDVQTT KHLFETLPIE ALKDSPDIGK
LQKITASEEE KGDVRHQKWI FETQPLEDIR KDKKEYTRTV KLEEVDRGDV KNYTHIFESN
NLIKFDASHK IEVEGVTRGA VELNKSLFET TPLYAIQDPL GKYHQVKTVQ QEEIVRGDVR
SCRWLFETRP IDQFDESIHK FQIIRGISAQ EIQTGNVKSA KWLFETQPLD SIKYFSDVEE
TESKTEQTRD IVKGDVKTCK WLFETQPMES LYEKVSLMTS SEEIHKGDVK TCTWLFETQP
LDTIKDDSET AVKLQTVKQE EIQGGDVRTA CFLFETENLD SIQGEEVKEI KPVEMDIQAG
DVSSMRYKFE NQSLDSISSS SEEVLKKIKT LKTEDIQKGN VLNCRWLFEN QPIDKIKESQ
EGDECVKTVT DIQGGDVRKG CFIFETFSLD EIKEESDYIS TKKTITEEVI QGDVKSYRML
FETQPLYAIQ DREGSYHEVT TVKKEEVIHG DVRGTRWLFE TKPLDSINKS ETVYVIKSVT
QEDIQKGDVS SVRYRFETQP LDQISEESHN IMPSIDHIQG GNVKTSRQFF ESENFDKNNY
IRTVSVNEIQ KGNVKTSTWL FETHTMDELR GEGLEYENIK TVTQEDVQKG DVKQAVWLFE
NRTFDSIMEA HKGITKMTKE EIPPSDVKTT TWLFETTPLH EFNETRVEKI EIIGKSIKET
LEDLYSQKVI QAPGIIIEAD EIGDVRMAKY KLMNQASPEI QKEEIIRADL RNIMVNLLSK
RDCTEREILI SEEEKGNVNL TKTQLLNRST EFHAEKEEIV KGDVQQAIKN LFSEERSVKK
GILIQEDEKG DINMTIYCLL HENDGDTIER EEVIGGDVKR TIHNLLSSTS NNKISERAKI
DASERGNVQF FTTCIEAGAL DYLKQLHTES NETLTAKKQE GEKEIIGGDV EGTKLLLKKR
QSLVERTVSE TDIIPGDVHN TVKVFMTEPQ STFGKIPKEE IIKGDLTSTL NSLSQAVNQK
TVTKTEEIIK GNMLATLKSL KESSHRWKES KQPDAIPGDI EKAIECLEKA TNTKTEILKK
ELLKDDLETS LRSLKEAQRS FKEVHKEGVI KKDAKAVMAG SSGEQKTDIH QVAVQRNKNS
LLQPKPGPFE PAAKWQGGAD TLSQTMGKSC HGNLVEERTE VNLPKAPKGT VKIVIDREQN
NDALEKSLRR LSNSHHKSNV LESGDKTGVW TDTTGEQHLR DEYMSRQLTS TVSVKNNLTT
KESDRAVREL KKDDVFNSIQ SAGKTVGKQQ TYELRNDHQK MEGFHIKSPK KTKNIKILTD
TQSSKPSPTQ HPVSMPVGGT YDLSGDFQKQ TLLKQETKYS NKDIKKKNIN LQPMWQLLPV
EQDTSNVTEM KVSEKSHNTF KATNKKRETD VHLKSQDFLM KTNTSTGLKM AMERSLNPIN
FNPENNVKES ECPLPPPSPP PPPPSNASSE IEFPLPPPPP LMMFPEKNGF LPSLSTEKIK
AEFESFPGLP LPPPPVDEKS ERESSSMFLP PPPPPTPSQK PAHLLSSSAP EKHSGDFMQQ
YSQKEASNSQ NSQAKIITGK TGVLPPPTLP KPKLPKHIKD NKNDFSPKVE LATSLSDMEC
KITTSKDQKK VMVMTSSEHT ETKQNVISKS LDERKQLSID SANCLSHTVP GTSAPRKKQI
APLIKSHSFP ESSGQQNPKP YMRKFKTPLM IAEEKYRQQK EEIEKQKQES SYYNIVKTQS
QNQHITEVEK EMPLQKTNEE VSLSGIDSEC TVVQPSPGSQ SNARILGVCS DNQLSTTSPE
TVAAKRLHHV LAASEDKDKM KKEVLQSSRD IMQSKSACEI KQSHQECSTQ QTQQKKYLEQ
LHLPQSKPIS PNFKVKTIKL PTLDHTLNET DHSYESHKQQ SEIDVQTFTK KQYLKTKKTE
ASTECSHKQS LAERHYQLPK KEKRVTVQLP TESIQKNQED KLKMVPRKQR EFSGSDRGKL
PGSEEKNQGP SMIGRKEERL ITERKHEHLK NKSAPKVVKQ KVIDAHLDSQ TQNFQQTQIQ
TAESKAEHKK LPQPYNSLQE EKCLEVKGIQ EKQVFSNTKD SKQEITQNKS FFSSVKESQR
DDGKGALNIV EFLRKREELQ QILSRVKQFE AEPNKSGLKT FQTLLNTIPG WLISEDKREY
AVHIAMENNL EKVKEEITHI KTQAEDMLVS YENIIQTAMM SSKTGKPGNK PTSLDETSSK
VSNVHVSNNK NSEQKENKIA KEKTVQHQVA AHHEATVRSH VKTHQEIKLD DSNIPPPSLK
TRPPSPTFIT IESTARRTEN PTKNELSQSP KKDSYVEPPP RRPMSQKSEI HRANTSPSPP
RSRSEQLVRL KDTTAKLSKG AIPCPAATPV PIVEKRSEII MSPATLRRQI KIETRGRDSP
PTITIPVNIN HAASGSFRES VDAQEEIRKV EKRATYVHKD GLNSTDHMVP DTESYDAVEI
IRKVAVPPRL SEHTQRYEAA NRTVQMAENF VNDPENEINR WFREFEHGPV SEAKSNRRVY
AKGETNHNIQ QESRTFCKEE FGLTSLGNTS FTDFSCKHPR ELREKIPVKQ PRICSETRSL
SEHFSGMDAF ESQIVESKMK TSSSHSSEAG KSGCDFKHAP PTYEDVIAGH ILDISDSPKE
VRKNFQKTWQ ESGRVFKGLG YATADASATE MRTTFQEESA FISEAAAPRQ GNMYTLSKDS
LSNGVPSGRQ AEFS
