LRC41_HUMAN
ID LRC41_HUMAN Reviewed; 812 AA.
AC Q15345; A8K5G8; Q3MJ96; Q5TDF5; Q71RA8; Q9BSM0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Leucine-rich repeat-containing protein 41;
DE AltName: Full=Protein Muf1;
GN Name=LRRC41; Synonyms=MUF1; ORFNames=PP7759;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 45-812 (ISOFORM 3).
RC TISSUE=Brain, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-609.
RC TISSUE=Brain, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-812 (ISOFORM 2), AND VARIANT
RP ILE-609.
RC TISSUE=Endometrium;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-812 (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 249-812 (ISOFORM 2).
RC TISSUE=Tonsil;
RA Kreideweiss S., Delany-Heiken P., Nordheim A., Ruhlmann A.C.C.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH CUL5.
RX PubMed=11384984; DOI=10.1074/jbc.m103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can
RT assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [9]
RP FUNCTION IN AN E3 UBIQUITIN LIGASE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH CUL5; RNF7; ELOB AND ELOC.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C.,
RA Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1
RT and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-276; SER-326;
RP THR-327; SER-357 AND SER-373, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Probable substrate recognition component of an ECS (Elongin
CC BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000269|PubMed:15601820}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of an E3 ubiquitin-protein ligase complex with Elongin BC
CC (ELOB and ELOC), RBX1 and CUL5. Component of a probable ECS(LRRC41)
CC complex which contains CUL5, RNF7/RBX2, Elongin BC and LRRC41.
CC Interacts with CUL5, RNF7, ELOB and ELOC. {ECO:0000269|PubMed:11384984,
CC ECO:0000269|PubMed:15601820}.
CC -!- INTERACTION:
CC Q15345; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-721408, EBI-3867333;
CC Q15345; Q5TD97: FHL5; NbExp=3; IntAct=EBI-721408, EBI-750641;
CC Q15345; Q15323: KRT31; NbExp=3; IntAct=EBI-721408, EBI-948001;
CC Q15345; O76011: KRT34; NbExp=3; IntAct=EBI-721408, EBI-1047093;
CC Q15345; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-721408, EBI-9996449;
CC Q15345; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-721408, EBI-11962084;
CC Q15345; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-721408, EBI-12275818;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q15345-2; Sequence=Displayed;
CC Name=3;
CC IsoId=Q15345-3; Sequence=VSP_009234, VSP_009235;
CC -!- DOMAIN: The Elongin BC complex binding domain is also known as BC-box
CC with the consensus [APST]-L-x(3)-C-x(3)-[AILV].
CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ15266.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ15266.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA60013.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD97609.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 3]:
CC Sequence=BAC86308.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86308.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK125827; BAC86308.1; ALT_SEQ; mRNA.
DR EMBL; AK291283; BAF83972.1; -; mRNA.
DR EMBL; AK297596; BAG59981.1; -; mRNA.
DR EMBL; AL121602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL122001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06927.1; -; Genomic_DNA.
DR EMBL; BC004953; AAH04953.2; -; mRNA.
DR EMBL; BC101522; AAI01523.1; -; mRNA.
DR EMBL; BC101524; AAI01525.1; -; mRNA.
DR EMBL; BX537366; CAD97609.1; ALT_FRAME; mRNA.
DR EMBL; AF370430; AAQ15266.1; ALT_SEQ; mRNA.
DR EMBL; X86018; CAA60013.1; ALT_FRAME; mRNA.
DR CCDS; CCDS533.1; -. [Q15345-2]
DR PIR; S52797; S52797.
DR RefSeq; NP_006360.3; NM_006369.4. [Q15345-2]
DR AlphaFoldDB; Q15345; -.
DR SMR; Q15345; -.
DR BioGRID; 115752; 77.
DR IntAct; Q15345; 24.
DR MINT; Q15345; -.
DR STRING; 9606.ENSP00000477792; -.
DR iPTMnet; Q15345; -.
DR PhosphoSitePlus; Q15345; -.
DR BioMuta; LRRC41; -.
DR DMDM; 150421588; -.
DR EPD; Q15345; -.
DR jPOST; Q15345; -.
DR MassIVE; Q15345; -.
DR MaxQB; Q15345; -.
DR PaxDb; Q15345; -.
DR PeptideAtlas; Q15345; -.
DR PRIDE; Q15345; -.
DR ProteomicsDB; 60534; -. [Q15345-2]
DR ProteomicsDB; 60535; -. [Q15345-3]
DR Antibodypedia; 32783; 141 antibodies from 28 providers.
DR DNASU; 10489; -.
DR Ensembl; ENST00000343304.10; ENSP00000343298.6; ENSG00000132128.18. [Q15345-2]
DR Ensembl; ENST00000617190.5; ENSP00000477792.1; ENSG00000132128.18. [Q15345-2]
DR GeneID; 10489; -.
DR KEGG; hsa:10489; -.
DR MANE-Select; ENST00000617190.5; ENSP00000477792.1; NM_006369.5; NP_006360.3.
DR UCSC; uc001cpn.4; human. [Q15345-2]
DR CTD; 10489; -.
DR DisGeNET; 10489; -.
DR GeneCards; LRRC41; -.
DR HGNC; HGNC:16917; LRRC41.
DR HPA; ENSG00000132128; Low tissue specificity.
DR MIM; 618753; gene.
DR neXtProt; NX_Q15345; -.
DR OpenTargets; ENSG00000132128; -.
DR PharmGKB; PA142671529; -.
DR VEuPathDB; HostDB:ENSG00000132128; -.
DR eggNOG; ENOG502R5T0; Eukaryota.
DR GeneTree; ENSGT00390000015908; -.
DR HOGENOM; CLU_021836_0_0_1; -.
DR InParanoid; Q15345; -.
DR OMA; PECRFRV; -.
DR OrthoDB; 322569at2759; -.
DR PhylomeDB; Q15345; -.
DR TreeFam; TF335481; -.
DR PathwayCommons; Q15345; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q15345; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10489; 24 hits in 1115 CRISPR screens.
DR ChiTaRS; LRRC41; human.
DR GeneWiki; LRRC41; -.
DR GenomeRNAi; 10489; -.
DR Pharos; Q15345; Tbio.
DR PRO; PR:Q15345; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15345; protein.
DR Bgee; ENSG00000132128; Expressed in right uterine tube and 201 other tissues.
DR ExpressionAtlas; Q15345; baseline and differential.
DR Genevisible; Q15345; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR026137; Leu_rpt_41.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR15354; PTHR15354; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..812
FT /note="Leucine-rich repeat-containing protein 41"
FT /id="PRO_0000096645"
FT REPEAT 487..507
FT /note="LRR 1"
FT REPEAT 518..530
FT /note="LRR 2"
FT REPEAT 531..555
FT /note="LRR 3"
FT REPEAT 613..635
FT /note="LRR 4"
FT REPEAT 636..659
FT /note="LRR 5"
FT REPEAT 701..728
FT /note="LRR 6"
FT REPEAT 731..752
FT /note="LRR 7"
FT REGION 45..54
FT /note="Interaction with Elongin BC complex"
FT /evidence="ECO:0000250"
FT REGION 267..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 716..729
FT /note="NAGLLALADVFSED -> GGQTLGRERGKELG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009234"
FT VAR_SEQ 730..812
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009235"
FT VARIANT 609
FT /note="V -> I (in dbSNP:rs11542623)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_051117"
FT CONFLICT 429
FT /note="E -> K (in Ref. 6; AAQ15266)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="A -> S (in Ref. 7; BAC86308)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="M -> I (in Ref. 5; CAD97609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 88650 MW; 9356F26D014B436A CRC64;
MAAPEAWRAR SCWFCEVAAA TTMEATSREA APAKSSASGP NAPPALFELC GRAVSAHMGV
LESGVWALPG PILQSILPLL NIYYLERIEE TALKKGLSTQ AIWRRLWDEL MKTRPSSLES
VTCWRAKFME AFFSHVLRGT IDVSSDRRLC DQRFSPLLHS SRHVRQLTIC NMLQGATELV
AEPNRRVLET LASSLHTLKF RHLLFSDVAA QQSLRQLLHQ LIHHGAVSQV SLYSWPVPES
ALFILILTMS AGFWQPGPGG PPCRLCGEAS RGRAPSRDEG SLLLGSRRPR RDAAERCAAA
LMASRRKSEA KQMPRAAPAT RVTRRSTQES LTAGGTDLKR ELHPPATSHE APGTKRSPSA
PAATSSASSS TSSYKRAPAS SAPQPKPLKR FKRAAGKKGA RTRQGPGAES EDLYDFVFIV
AGEKEDGEEM EIGEVACGAL DGSDPSCLGL PALEASQRFR SISTLELFTV PLSTEAALTL
CHLLSSWVSL ESLTLSYNGL GSNIFRLLDS LRALSGQAGC RLRALHLSDL FSPLPILELT
RAIVRALPLL RVLSIRVDHP SQRDNPGVPG NAGPPSHIIG DEEIPENCLE QLEMGFPRGA
QPAPLLCSVL KASGSLQQLS LDSATFASPQ DFGLVLQTLK EYNLALKRLS FHDMNLADCQ
SEVLFLLQNL TLQEITFSFC RLFEKRPAQF LPEMVAAMKG NSTLKGLRLP GNRLGNAGLL
ALADVFSEDS SSSLCQLDIS SNCIKPDGLL EFAKRLERWG RGAFGHLRLF QNWLDQDAVT
AREAIRRLRA TCHVVSDSWD SSQAFADYVS TM
