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WASH complex subunit 2

 WASC2_CRIGR             Reviewed;        1317 AA.
Q91Y25;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 45.
RecName: Full=WASH complex subunit 2 {ECO:0000250|UniProtKB:Q6PGL7};
Name=Washc2 {ECO:0000250|UniProtKB:Q6PGL7}; Synonyms=Fam21;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
Bair C.-H., Chang W.;
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Acts at least in part as component of the WASH core
complex whose assembly at the surface of endosomes inhibits WASH
nucleation-promoting factor (NPF) activity in recruiting and
activating the Arp2/3 complex to induce actin polymerization and
is involved in the fission of tubules that serve as transport
intermediates during endosome sorting. Mediates the recruitment of
the WASH core complex to endosome membranes via binding to
phospholipids and VPS35 of the retromer CSC. Mediates the
recruitment of the F-actin-capping protein dimer to the WASH core
complex probably promoting localized F-actin polymerization needed
for vesicle scission. Via its C-terminus binds various
phospholipids, most strongly phosphatidylinositol 4-phosphate
(PtdIns-(4)P), phosphatidylinositol 5-phosphate (PtdIns-(5)P) and
phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2). Involved
in the endosome-to-plasma membrane trafficking and recycling of
SNX27-retromer-dependent cargo proteins, such as GLUT1. Required
for the association of DNAJC13, SDCCAG3, ANKRD50 with retromer CSC
subunit VPS35. Required for the endosomal recruitment of CCC
complex subunits COMMD1, CCDC93 and C16orf62 homolog (By
similarity). {ECO:0000250|UniProtKB:Q9Y4E1}.
-!- SUBUNIT: Component of the WASH core complex also described as WASH
regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4
and WASHC5; in the complex interacts (via N-terminus) directly
with WASHC1. The WASH core complex associates via WASHC2 with the
F-actin-capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3
and CAPZB) in a transient or substoichiometric manner which was
initially described as WASH complex. Interacts with VPS35;
mediates the association with the retromer CSC complex. Interacts
with FKBP15. Interacts with CCDC93, CCDC22, C16orf62 homolog;
indicative for an association of the WASH core complex with the
CCC complex (By similarity). Directly interacts with TBC1D23 (By
similarity). {ECO:0000250|UniProtKB:Q641Q2,
ECO:0000250|UniProtKB:Q9Y4E1}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000250|UniProtKB:Q9Y4E1}. Cell membrane
{ECO:0000250|UniProtKB:Q9Y4E1}.
-!- DOMAIN: The LFa (leucine-phenylalanine-acidic) motif bind directly
to VPS35 of retromer CSC; adjacent motifs can act cooperatively to
bind multiple CSCs, although there is significant variability in
the affinities of different motifs for retromer.
{ECO:0000250|UniProtKB:Q9Y4E1}.
-!- SIMILARITY: Belongs to the FAM21 family. {ECO:0000305}.
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EMBL; AF371373; AAK53434.1; -; mRNA.
RefSeq; NP_001231222.1; NM_001244293.1.
PRIDE; Q91Y25; -.
GeneID; 100689255; -.
KEGG; cge:100689255; -.
CTD; 28006; -.
HOVERGEN; HBG055529; -.
KO; K18462; -.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
InterPro; IPR027308; FAM21.
InterPro; IPR029341; FAM21/CAPZIP.
PANTHER; PTHR21669:SF24; PTHR21669:SF24; 1.
Pfam; PF15255; CAP-ZIP_m; 1.
2: Evidence at transcript level;
Cell membrane; Endosome; Membrane; Phosphoprotein; Protein transport;
Transport.
CHAIN 1 1317 WASH complex subunit 2.
/FTId=PRO_0000317432.
REGION 1 219 Sufficient for interaction with WASHC3,
WASHC4 and WASHC5; required for
interaction with WASHC1.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 348 582 Sufficient for interaction with CCDC93.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 349 1317 Interaction with VPS35.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 912 1317 Interaction with phospholipids.
{ECO:0000250|UniProtKB:Q9Y4E1}.
REGION 1004 1022 Required for interaction with F-actin-
capping protein subunit alpha (CAPZA1 or
CAPZA2 or CAPZA3).
{ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 358 368 LFa 1. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 433 445 LFa 2. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 464 473 LFa 3. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 519 530 LFa 4. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 554 565 LFa 5. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 599 611 LFa 6. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 646 657 LFa 7. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 673 685 LFa 8. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 815 823 LFa 9. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 832 838 LFa 10. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 854 864 LFa 11. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1107 1114 LFa 12. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1147 1161 LFa 13. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1177 1185 LFa 14. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1210 1216 LFa 15. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1238 1246 LFa 16. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1266 1275 LFa 17. {ECO:0000250|UniProtKB:Q9Y4E1}.
MOTIF 1306 1314 LFa 18. {ECO:0000250|UniProtKB:Q9Y4E1}.
COMPBIAS 221 228 Poly-Glu.
COMPBIAS 435 442 Poly-Asp.
COMPBIAS 676 679 Poly-Asp.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 323 323 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 601 601 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 602 602 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 710 710 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 763 763 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000250|UniProtKB:Q641Q2}.
MOD_RES 1047 1047 Phosphoserine.
{ECO:0000250|UniProtKB:Q80X08}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:Q641Q2}.
MOD_RES 1092 1092 Phosphoserine.
{ECO:0000250|UniProtKB:Q641Q2}.
MOD_RES 1152 1152 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 1156 1156 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
MOD_RES 1316 1316 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PGL7}.
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


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