WASC2_CRIGR
ID WASC2_CRIGR Reviewed; 1317 AA.
AC Q91Y25;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=WASH complex subunit 2 {ECO:0000250|UniProtKB:Q6PGL7};
GN Name=Washc2 {ECO:0000250|UniProtKB:Q6PGL7}; Synonyms=Fam21;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Bair C.-H., Chang W.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a component of the WASH core complex that functions
CC as a nucleation-promoting factor (NPF) at the surface of endosomes,
CC where it recruits and activates the Arp2/3 complex to induce actin
CC polymerization, playing a key role in the fission of tubules that serve
CC as transport intermediates during endosome sorting. Mediates the
CC recruitment of the WASH core complex to endosome membranes via binding
CC to phospholipids and VPS35 of the retromer CSC. Mediates the
CC recruitment of the F-actin-capping protein dimer to the WASH core
CC complex probably promoting localized F-actin polymerization needed for
CC vesicle scission. Via its C-terminus binds various phospholipids, most
CC strongly phosphatidylinositol 4-phosphate (PtdIns-(4)P),
CC phosphatidylinositol 5-phosphate (PtdIns-(5)P) and phosphatidylinositol
CC 3,5-bisphosphate (PtdIns-(3,5)P2). Involved in the endosome-to-plasma
CC membrane trafficking and recycling of SNX27-retromer-dependent cargo
CC proteins, such as GLUT1. Required for the association of DNAJC13,
CC ENTR1, ANKRD50 with retromer CSC subunit VPS35. Required for the
CC endosomal recruitment of CCC complex subunits COMMD1, CCDC93 and
CC C16orf62 homolog (By similarity). {ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SUBUNIT: Component of the WASH core complex also described as WASH
CC regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4 and
CC WASHC5; in the complex interacts (via N-terminus) directly with WASHC1.
CC The WASH core complex associates via WASHC2 with the F-actin-capping
CC protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a
CC transient or substoichiometric manner which was initially described as
CC WASH complex. Interacts with VPS35; mediates the association with the
CC retromer CSC complex. Interacts with FKBP15. Interacts with CCDC93,
CC CCDC22, C16orf62 homolog; indicative for an association of the WASH
CC core complex with the CCC complex (By similarity). Directly interacts
CC with TBC1D23 (By similarity). {ECO:0000250|UniProtKB:Q641Q2,
CC ECO:0000250|UniProtKB:Q9Y4E1}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y4E1}.
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 -!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
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DR EMBL; AF371373; AAK53434.1; -; mRNA.
DR RefSeq; NP_001231222.1; NM_001244293.1.
DR AlphaFoldDB; Q91Y25; -.
DR SMR; Q91Y25; -.
DR STRING; 10029.NP_001231222.1; -.
DR PRIDE; Q91Y25; -.
DR GeneID; 100689255; -.
DR KEGG; cge:100689255; -.
DR CTD; 28006; -.
DR eggNOG; ENOG502QTIY; Eukaryota.
DR OrthoDB; 131637at2759; -.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell membrane; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Transport.
FT CHAIN 1..1317
FT /note="WASH complex subunit 2"
FT /id="PRO_0000317432"
FT REGION 1..219
FT /note="Sufficient for interaction with WASHC3, WASHC4 and
FT WASHC5; required for interaction with WASHC1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 201..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..582
FT /note="Sufficient for interaction with CCDC93"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 349..1317
FT /note="Interaction with VPS35"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 667..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1317
FT /note="Interaction with phospholipids"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 960..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1022
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 1119..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 358..368
FT /note="LFa 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 433..445
FT /note="LFa 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 464..473
FT /note="LFa 3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 519..530
FT /note="LFa 4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 554..565
FT /note="LFa 5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 599..611
FT /note="LFa 6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 646..657
FT /note="LFa 7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 673..685
FT /note="LFa 8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 815..823
FT /note="LFa 9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 832..838
FT /note="LFa 10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 854..864
FT /note="LFa 11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1107..1114
FT /note="LFa 12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1147..1161
FT /note="LFa 13"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1177..1185
FT /note="LFa 14"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1210..1216
FT /note="LFa 15"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1238..1246
FT /note="LFa 16"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1266..1275
FT /note="LFa 17"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1306..1314
FT /note="LFa 18"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT COMPBIAS 220..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1019
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 1316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
SQ SEQUENCE 1317 AA; 144930 MW; 5BCEC0B634B277A2 CRC64;
MNRTSPDSER PPGSEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI
KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQALKA EAEKSEQEKT
REQKEVDLIP KVREAVNYGL QVLDSAFEQL DIKAGNSDSE EEDANERVEL ILEPKDLYID
RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EEEKEEEESD EDFASRSDND
QNQHTTRMSD EEEDDDGDLF ADSEKEGDDI EDIEENTKSK RPTSFADELA ARIKGDMSNQ
LKEEQIADGK PQKTMKEKKE KRTPPDDEED ILFPPPKLTD EDFSPFGSRG GLFSGQGLFD
DEDESDLFRE TSRDRPAQAP VSEESSSPKP GKKIPAGAVS VFLDTSAPSL KEFQKHEQPT
PGKNPHLPTP AGLFDDNDDD DDNFFVPSCN KPPKTDKVKS TSIIFDDEEG DLFREKPAPL
PVASVSQADE NTTRADKTIT LPSSKNPKLV SETKTQKGLF SDEEDSEDLF SSQNSSKSKS
ASLLSSQLPT SGSLFGDEDE EDNLFGSAPA KKQVSSQQPQ SQEKPKPSEQ PKKKASALLF
SSDEEDQWNI TDSHTKLATD RKSKGELWDS GTIQGQEVKA VKKTNLFEED DDEADLFAIA
KDSQKKTQRT SLLFEDDDDS GSSLFGFPPA SVPPATMKKE SISKVPSLFS DEEENEVPSR
VKSVDVKVGN GKEADVAKVT EKEGLLTASD QEAAGPSDLF SSSPLDKGTK GRTKTVLSLF
DEEEDKVEDQ SNTHVSKNDA EKGLKTDGRP KSTGVFQDEE LLFSHKLQKD NDPDVDLFAG
TKKTRVSVPL DGSLFGDDED YDLFSSAKTQ PVVPEKKGAL KKDRPVSLKN EEAPESTEGS
KEKSLWKAET PQDSSGLTPF KSREPSSRIG KIQANLAINP AALLPTAALQ IPGTKPALCE
LAFPSSEPGR SHGPESVPTL AGSEEAGVSF DLPAQADTLH SANKSRVKVR GKRRPQTRAA
RRLAAQESSE SEDMSVSRGP VAQLASSPIL PNGHQPHLQP RMASGEISSE KAMAPAAPPW
ESGPALSAVD RSFFVASLPQ TGNEADLFDS GDIFPKSIGS QSMEGTKVKA AETPAHLSGG
SKEKSLVFPA LSEASSTDDL FQTVKPRPAK KRNPFPLLED EDDLFADRKG KKNELKSDSH
QDIISKTQDI FEDDIFATEA VKPFQKKREK ERTLEPNLFD DNIDIFADLN VKPKEKSKKK
VEAKSVFDDD TDDIFSSGLQ AKKSKPKSQS AEATSELRSD HKVSNIFDDP LNAFGSQ
