WAC2A_HUMAN
ID WAC2A_HUMAN Reviewed; 1341 AA.
AC Q641Q2; A2A3S2; A2A3U6; Q5SNT6; Q6DHY0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=WASH complex subunit 2A {ECO:0000312|HGNC:HGNC:23416};
GN Name=WASHC2A {ECO:0000312|HGNC:HGNC:23416};
GN Synonyms=FAM21A {ECO:0000312|HGNC:HGNC:23416},
GN FAM21B {ECO:0000312|HGNC:HGNC:23416};
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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Spleen;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539; SER-1087 AND SER-1114,
RP AND IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539; SER-1087 AND SER-1114,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-1114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-1054, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
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).
RN [10]
RP FUNCTION, AND INTERACTION WITH CCDC93; CCDC22 AND VPS35L.
RX PubMed=25355947; DOI=10.1091/mbc.e14-06-1073;
RA Phillips-Krawczak C.A., Singla A., Starokadomskyy P., Deng Z.,
RA Osborne D.G., Li H., Dick C.J., Gomez T.S., Koenecke M., Zhang J.S.,
RA Dai H., Sifuentes-Dominguez L.F., Geng L.N., Kaufmann S.H., Hein M.Y.,
RA Wallis M., McGaughran J., Gecz J., van de Sluis B., Billadeau D.D.,
RA Burstein E.;
RT "COMMD1 is linked to the WASH complex and regulates endosomal trafficking
RT of the copper transporter ATP7A.";
RL Mol. Biol. Cell 26:91-103(2015).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28892079; DOI=10.1038/ncb3610;
RA McNally K.E., Faulkner R., Steinberg F., Gallon M., Ghai R., Pim D.,
RA Langton P., Pearson N., Danson C.M., Naegele H., Morris L.L., Singla A.,
RA Overlee B.L., Heesom K.J., Sessions R., Banks L., Collins B.M., Berger I.,
RA Billadeau D.D., Burstein E., Cullen P.J.;
RT "Retriever is a multiprotein complex for retromer-independent endosomal
RT cargo recycling.";
RL Nat. Cell Biol. 19:1214-1225(2017).
RN [12]
RP INTERACTION WITH TBC1D23.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
CC -!- FUNCTION: Acts at least in part as component of the WASH core complex
CC whose assembly at the surface of endosomes inhibits WASH nucleation-
CC promoting factor (NPF) activity in recruiting and activating the Arp2/3
CC complex to induce actin polymerization and is involved in the fission
CC of tubules that serve as transport intermediates during endosome
CC sorting. Mediates the recruitment of the WASH core complex to endosome
CC membranes via binding to phospholipids and VPS35 of the retromer CSC.
CC Mediates the recruitment of the F-actin-capping protein dimer to the
CC WASH core complex probably promoting localized F-actin polymerization
CC needed for vesicle scission. Via its C-terminus binds various
CC phospholipids, most strongly phosphatidylinositol 4-phosphate (PtdIns-
CC (4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and
CC phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the
CC endosome-to-plasma membrane trafficking and recycling of SNX27-
CC retromer-dependent cargo proteins, such as GLUT1. Required for the
CC association of DNAJC13, ENTR1, ANKRD50 with retromer CSC subunit VPS35.
CC Required for the endosomal recruitment of CCC complex subunits COMMD1
CC and CCDC93 as well as the retriever complex subunit VPS35L.
CC {ECO:0000269|PubMed:25355947, ECO:0000269|PubMed:28892079}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex (SHRC) composed of WASH (WASHC1, WASH2P or WASH3P),
CC WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5; in the complex
CC interacts (via N-terminus) directly with WASHC1. The WASH core complex
CC associates with the F-actin-capping protein dimer (formed by CAPZA1,
CC CAPZA2 or CAPZA3 and CAPZB) in a transient or substoichiometric manner
CC which was initially described as WASH complex. Interacts with VPS35;
CC mediates the association with the retromer CSC complex. Interacts with
CC FKBP15. Interacts with CCDC93, CCDC22, VPS35L; indicative for an
CC association of the WASH core complex with the CCC and retriever
CC complexes (PubMed:25355947). Directly interacts with TBC1D23
CC (PubMed:29084197). {ECO:0000250|UniProtKB:Q9Y4E1,
CC ECO:0000269|PubMed:25355947, ECO:0000269|PubMed:29084197}.
CC -!- INTERACTION:
CC Q641Q2; O60826: CCDC22; NbExp=6; IntAct=EBI-2870155, EBI-3943153;
CC Q641Q2; Q567U6: CCDC93; NbExp=9; IntAct=EBI-2870155, EBI-1104769;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:28892079}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q641Q2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q641Q2-2; Sequence=VSP_030948;
CC -!- DOMAIN: The LFa (leucine-phenylalanine-acidic) motif bind directly to
CC VPS35 of retromer CSC; adjacent motifs can act cooperatively to bind
CC multiple CSCs, although there is significant variability in the
CC affinities of different motifs for retromer.
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- MISCELLANEOUS: In human, WASHC2 has undergone evolutionary duplication,
CC with 2 highly homologous family members WASHC2A and WASHC2C.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
CC -!- CAUTION: A WASHC2C construct with WASHC2A-specific sequence insertions
CC has been used in a number of experiments; the results are included in
CC the WASHC2C entry. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI17187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL442003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954360; CAI17187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC075815; AAH75815.1; -; mRNA.
DR EMBL; BC082258; AAH82258.2; -; mRNA.
DR CCDS; CCDS41527.1; -. [Q641Q2-1]
DR CCDS; CCDS76303.1; -. [Q641Q2-2]
DR RefSeq; NP_001005751.1; NM_001005751.2. [Q641Q2-1]
DR RefSeq; NP_001278327.1; NM_001291398.1. [Q641Q2-2]
DR AlphaFoldDB; Q641Q2; -.
DR SMR; Q641Q2; -.
DR BioGRID; 132390; 79.
DR ComplexPortal; CPX-1172; WASH complex, variant WASHC1/WASHC2A.
DR ComplexPortal; CPX-1173; WASH complex, variant WASH2P/WASHC2A.
DR ComplexPortal; CPX-1174; WASH complex, variant WASH3P/WASHC2A.
DR ComplexPortal; CPX-1175; WASH complex, variant WASH4P/WASHC2A.
DR ComplexPortal; CPX-1176; WASH complex, variant WASH6P/WASHC2A.
DR CORUM; Q641Q2; -.
DR IntAct; Q641Q2; 43.
DR MINT; Q641Q2; -.
DR STRING; 9606.ENSP00000282633; -.
DR TCDB; 9.A.3.1.2; the sorting nexin27 (snx27)-retromer assembly apparatus (retromeraa) family.
DR iPTMnet; Q641Q2; -.
DR PhosphoSitePlus; Q641Q2; -.
DR BioMuta; WASHC2A; -.
DR DMDM; 166971555; -.
DR EPD; Q641Q2; -.
DR jPOST; Q641Q2; -.
DR MassIVE; Q641Q2; -.
DR MaxQB; Q641Q2; -.
DR PaxDb; Q641Q2; -.
DR PeptideAtlas; Q641Q2; -.
DR PRIDE; Q641Q2; -.
DR ProteomicsDB; 63762; -.
DR ProteomicsDB; 65910; -. [Q641Q2-1]
DR ProteomicsDB; 65911; -. [Q641Q2-2]
DR Antibodypedia; 76770; 18 antibodies from 6 providers.
DR DNASU; 387680; -.
DR Ensembl; ENST00000282633.10; ENSP00000282633.5; ENSG00000099290.17. [Q641Q2-1]
DR Ensembl; ENST00000351071.11; ENSP00000344037.6; ENSG00000099290.17. [Q641Q2-2]
DR GeneID; 387680; -.
DR KEGG; hsa:387680; -.
DR MANE-Select; ENST00000282633.10; ENSP00000282633.5; NM_001005751.3; NP_001005751.1.
DR UCSC; uc001jjb.4; human. [Q641Q2-1]
DR CTD; 387680; -.
DR GeneCards; WASHC2A; -.
DR HGNC; HGNC:23416; WASHC2A.
DR HPA; ENSG00000099290; Low tissue specificity.
DR neXtProt; NX_Q641Q2; -.
DR PharmGKB; PA134902481; -.
DR VEuPathDB; HostDB:ENSG00000099290; -.
DR eggNOG; ENOG502QTIY; Eukaryota.
DR GeneTree; ENSGT00940000153997; -.
DR InParanoid; Q641Q2; -.
DR OMA; IHTIFYD; -.
DR PhylomeDB; Q641Q2; -.
DR TreeFam; TF329309; -.
DR PathwayCommons; Q641Q2; -.
DR SignaLink; Q641Q2; -.
DR BioGRID-ORCS; 387680; 11 hits in 1000 CRISPR screens.
DR ChiTaRS; WASHC2A; human.
DR GenomeRNAi; 387680; -.
DR Pharos; Q641Q2; Tdark.
DR PRO; PR:Q641Q2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q641Q2; protein.
DR Bgee; ENSG00000099290; Expressed in calcaneal tendon and 101 other tissues.
DR ExpressionAtlas; Q641Q2; baseline and differential.
DR Genevisible; Q641Q2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:1905394; F:retromer complex binding; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IC:ComplexPortal.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IC:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR InterPro; IPR029341; FAM21/CAPZIP.
DR Pfam; PF15255; CAP-ZIP_m; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1341
FT /note="WASH complex subunit 2A"
FT /id="PRO_0000317299"
FT REGION 1..220
FT /note="Sufficient for interaction with WASHC3, WASHC4 and
FT WASHC5; required for interaction with WASHC1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 202..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..742
FT /note="Required for interaction with CCDC22 and VPS35L"
FT /evidence="ECO:0000269|PubMed:25355947"
FT REGION 356..600
FT /note="Sufficient for interaction with CCDC93"
FT /evidence="ECO:0000269|PubMed:25355947"
FT REGION 357..1341
FT /note="Interaction with VPS35"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 422..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1341
FT /note="Interaction with phospholipids"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 988..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1047
FT /note="Required for interaction with F-actin-capping
FT protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 1302..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..378
FT /note="LFa 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 411..419
FT /note="LFa 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 450..463
FT /note="LFa 3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 482..491
FT /note="LFa 4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 537..548
FT /note="LFa 5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 572..583
FT /note="LFa 6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 617..629
FT /note="LFa 7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 664..674
FT /note="LFa 8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 690..702
FT /note="LFa 9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 726..738
FT /note="LFa 10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 803..817
FT /note="LFa 11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 839..847
FT /note="LFa 12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 856..862
FT /note="LFa 13"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 878..888
FT /note="LFa 14"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1129..1136
FT /note="LFa 15"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1171..1185
FT /note="LFa 16"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1201..1209
FT /note="LFa 17"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1234..1240
FT /note="LFa 18"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1262..1270
FT /note="LFa 19"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1290..1299
FT /note="LFa 20"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1330..1338
FT /note="LFa 21"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT COMPBIAS 231..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 938..958
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030948"
FT CONFLICT 342
FT /note="A -> T (in Ref. 1; CAI17187)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="G -> E (in Ref. 2; AAH75815)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="L -> S (in Ref. 1; CAI17187)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="G -> R (in Ref. 1; CAI17187)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="I -> T (in Ref. 2; AAH75815)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="H -> Y (in Ref. 2; AAH82258)"
FT /evidence="ECO:0000305"
FT CONFLICT 1198
FT /note="P -> T (in Ref. 1; CAI17187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1341 AA; 147184 MW; 8F0F755EB1493EA7 CRC64;
MMNRTTPDQE LAPASEPVWE RPWSVEEIRR SSQSWSLAAD AGLLQFLQEF SQQTISRTHE
IKKQVDGLIR ETKATDCRLH NVFNDFLMLS NTQFIENRVY DEEVEEPVLK AEAEKTEQEK
TREQKEVDLI PKVQEAVNYG LQVLDSAFEQ LDIKAGNSDS EEDDANGRVE LILEPKDLYI
DRPLPYLIGS KLFMEQEDVG LGELSSEEGS VGSDRGSIVD TEEEKEEEES DEDFAHHSDN
EQNRHTTQMS DEEEDDDGCD LFADSEKEEE DIEDIEENTR PKRSRPTSFA DELAARIKGD
AVGRVDEEPT TLPSGEAKPR KTLKEKKERR TPSDDEEDNL FAPPKLTDED FSPFGSGGGL
FSGGKGLFDD EDEESDLFTE APQDRQAGAS VKEESSSSKP GKKIPAGAVS VFLGDTDVFG
AASVPSMKEP QKPEQPTPRK SPYGPPPTGL FDDDDGDDDD DFFSAPHSKP SKTGKVQSTA
DIFGDEEGDL FKEKAVASPE ATVSQTDENK ARAEKKVTLS SSKNLKPSSE TKTQKGLFSD
EEDSEDLFSS QSASKLKGAS LLPGKLPTLV SLFDDEDEED NLFGGTAAKK QTLCLQAQRE
EKAKASELSK KKASALLFSS DEEDQWNIPA SQTHLASDSR SKGEPRDSGT LQSQEAKAVK
KTSLFEEDEE DDLFAIAKDS QKKTQRVSLL FEDDVDSGGS LFGSPPTSVP PATKKKETVS
EAPPLLFSDE EEKEAQLGVK SVDKKVESAK ESLKFGRTDV AESEKEGLLT RSAQETVKHS
DLFSSSSPWD KGTKPRTKTV LSLFDEEEDK MEDQNIIQAP QKEVGKGRDP DAHPKSTGVF
QDEELLFSHK LQKDNDPDVD LFAGTKKTKL LEPSVGSLFG DDEDDDLFSS AKSQPLVQEK
KRVVKKDHSV DSFKNQKHPE SIQGSKEKGI WKPETPQDSS GLAPFKTKEP STRIGKIQAN
LAINPAALLP TAASQISEVK PVLPELAFPS SEHRRSHGLE SVPVLPGSGE AGVSFDLPAQ
ADTLHSANKS RVKMRGKRRP QTRAARRLAA QESSETEDMS VPRGPIAQWA DGAISPNGHR
PQLRAASGED STEEALAAAA APWEGGPVPG VDRSPFAKSL GHSRGEADLF DSGDIFSTGT
GSQSVERTKP KAKIAENPAN PPVGGKAKSP MFPALGEASS DDDLFQSAKP KPAKKTNPFP
LLEDEDDLFT DQKVKKNETK SNSQQDVILT TQDIFEDDIF ATEAIKPSQK TREKEKTLES
NLFDDNIDIF ADLTVKPKEK SKKKVEAKSI FDDDMDDIFS SGIQAKTTKP KSRSAQAAPE
PRFEHKVSNI FDDPLNAFGG Q
