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   24-JAN-2024, entry version 139.
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}, FAM21B
GN   {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; 121.
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; 48.
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; 9606-ENSP00000282633; -.
DR   PeptideAtlas; Q641Q2; -.
DR   ProteomicsDB; 63762; -.
DR   ProteomicsDB; 65910; -. [Q641Q2-1]
DR   ProteomicsDB; 65911; -. [Q641Q2-2]
DR   Pumba; Q641Q2; -.
DR   Antibodypedia; 76770; 19 antibodies from 7 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   AGR; HGNC:23416; -.
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   OrthoDB; 12630at2759; -.
DR   PhylomeDB; Q641Q2; -.
DR   TreeFam; TF329309; -.
DR   PathwayCommons; Q641Q2; -.
DR   SignaLink; Q641Q2; -.
DR   BioGRID-ORCS; 387680; 23 hits in 1074 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 102 other cell types or tissues.
DR   ExpressionAtlas; Q641Q2; baseline and differential.
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; NAS: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; NAS: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; NAS:ComplexPortal.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   InterPro; IPR029341; FAM21/CAPZIP.
DR   PANTHER; PTHR21669; CAPZ-INTERACTING PROTEIN AND RELATED PROTEINS; 1.
DR   PANTHER; PTHR21669:SF38; WASH COMPLEX SUBUNIT 2A-RELATED; 1.
DR   Pfam; PF15255; CAP-ZIP_m; 1.
DR   Genevisible; Q641Q2; HS.
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
//