WASC2_PONAB
ID WASC2_PONAB Reviewed; 1340 AA.
AC Q5RDC1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=WASH complex subunit 2 {ECO:0000250|UniProtKB:Q6PGL7};
GN Name=Washc2 {ECO:0000250|UniProtKB:Q6PGL7}; Synonyms=FAM21;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 and retriever complexes subunits COMMD1
CC and CCDC93 as well as the retrievere complex subunit VPS35L.
CC {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
CC and WASHC5; in the complex interacts (via N-terminus) directly with
CC WASHC1. The WASH core complex associates 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, VPS35L; indicative for an association of the WASH core complex
CC with the CCC and retriever complexes (By similarity). Directly
CC interacts 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; CR857993; CAH90236.1; -; mRNA.
DR RefSeq; NP_001125099.1; NM_001131627.2.
DR AlphaFoldDB; Q5RDC1; -.
DR SMR; Q5RDC1; -.
DR PRIDE; Q5RDC1; -.
DR GeneID; 100171981; -.
DR KEGG; pon:100171981; -.
DR CTD; 28006; -.
DR eggNOG; ENOG502QTIY; Eukaryota.
DR InParanoid; Q5RDC1; -.
DR OrthoDB; 131637at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0036010; P:protein localization to endosome; ISS:UniProtKB.
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; Reference proteome;
KW Transport.
FT CHAIN 1..1340
FT /note="WASH complex subunit 2"
FT /id="PRO_0000186715"
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..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..599
FT /note="Sufficient for interaction with CCDC93"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 356..1340
FT /note="Interaction with VPS35"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 421..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1340
FT /note="Interaction with phospholipids"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT REGION 987..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1046
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 1301..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 366..377
FT /note="LFa 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 410..418
FT /note="LFa 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 449..462
FT /note="LFa 3"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 481..490
FT /note="LFa 4"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 536..547
FT /note="LFa 5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 571..582
FT /note="LFa 6"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 616..628
FT /note="LFa 7"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 663..673
FT /note="LFa 8"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 689..701
FT /note="LFa 9"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 725..737
FT /note="LFa 10"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 802..816
FT /note="LFa 11"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 838..846
FT /note="LFa 12"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 855..861
FT /note="LFa 13"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 877..887
FT /note="LFa 14"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1128..1135
FT /note="LFa 15"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1170..1184
FT /note="LFa 16"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1200..1208
FT /note="LFa 17"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1233..1239
FT /note="LFa 18"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1261..1269
FT /note="LFa 19"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1289..1298
FT /note="LFa 20"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT MOTIF 1329..1337
FT /note="LFa 21"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4E1"
FT COMPBIAS 249..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1043
FT /note="Basic 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 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X08"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q641Q2"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGL7"
SQ SEQUENCE 1340 AA; 146813 MW; 9B0C6D404AAB15DD CRC64;
MNRTTPDQEL APASEPVWER PWSVEEIRRS SQSWSLAADA GLLQFLQEFS QQTISRTHEI
KKQVDGLIRE TKATDCRLHN VFNDFLMLSN TQFIENRVYD EEVEEPVLKA EAEKTEQEKT
REQKEVDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANGRVEL ILEPKDLYID
RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDT EEEKEEEESD EDFAHHSDND
QNRNTTQMSD EEEDDDGCDL FADSEKEEED IEDIEEITRP KRNGPTSFAD ELAARIKGDA
VGRVDEEPTT LSSGEAKPRK TLKEKKERRT PSDDEEDNLF APPKLTDEDF SPFGSGGGLF
SGGKGLFDDE DEESDLFTEA PQDRQAGASV KEESSSSKPG KKIPAGAVSV FLGDTDVFGA
ASVPSLKEPQ KPEQPTPRKS PYFPPPTGLF DDDDGDDDDD FFSTPHSKPS KTGKVQSTAD
IFGDDEGDLF KEKAVTLPEA TVSQTDENKA RAEKKVSLPS SKNLKPSSET KTQKGLFSDE
EDSEDLFSSQ SASKLKGAPL LPGKLPTSVS LFEDEDEEDN LFGGTAAKRQ TLSLQAQGEE
KAKASELSKK KASALLFSSD EEDQWNIPAS QTHSASDSRS KGESRDSGTL QSQEAKAVKK
ASLFEEDEED DLFAIAKDSQ KKTQRVSLLF EDDVDSGGSL FGSPPTSVPP ATTKKETVSE
APPLLFSDEE EKEAQLGVKP VDKKVESAKE SLKFGRTDVA ESEKEGLLTR SAQEAVKHSD
LFSSSSPLDK GTKPRTKTVL SLFDEEEDKM EDQNTIQAPQ KEVGKGRDPD ARPKSTGVFQ
DEELLFSHKL QKDNDPDVDL FAGTKKTKLL EPSVGSLFGD DEDDDLFSSA KSQPLVQEKK
RVVKKDYSVD SVKNQKHPET IQGIKEKGIW KPETPQDSSG LAPFKTKEPS TRIGKIQANL
AINPAALLPT AASQISEVKP VLPELAFPSS EHRRSHGLES VPVLPGSGEA GVSFDLPAQA
DTLHSANKSR VKMRGKRRPQ TRAARRLAAQ ESSEAEDMSV PRGPIAQWAD GTISPNGHRP
QLRAASGEDS TEEALAAAAA PWEGGPVPGV DRSPFAKSLG HSRGEADLFD SGDIFSTGTG
SQSEERTKPK AKIAENLANP PVGGKAKSPM FPALGEASSD DDLFQSAKPK PAKKTNPFPL
LEDEDDLFTD QKVKKNETKS DSQQDVISTT QDIFEDDIFA TEAIKPSQKT REKEKTLESN
LFDDNIDIFA DLTVKPKEKS KKKVEAKSIF DDDMDDIFSS GIQAKTAKPK SRSAQAAPEP
RFEHKVSNIF DDPLNAFGGQ
