ID   WASC5_PONAB             Reviewed;        1159 AA.
AC   Q5R5P0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=WASH complex subunit 5 {ECO:0000250|UniProtKB:Q12768};
DE   AltName: Full=WASH complex subunit strumpellin {ECO:0000305};
GN   Name=WASHC5 {ECO:0000250|UniProtKB:Q12768};
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. May be involved in
CC       axonal outgrowth. Involved in cellular localization of ADRB2. Involved
CC       in cellular trafficking of BLOC-1 complex cargos such as ATP7A and
CC       VAMP7 (By similarity). {ECO:0000250|UniProtKB:Q12768}.
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. The WASH core
CC       complex associates via WASHC2 with the F-actin-capping protein dimer
CC       (formed by CAPZA1, CAPZA2 or CAPZA3 and CAPZB) in a transient or
CC       substoichiometric manner which was initially described as WASH complex.
CC       Interacts with VCP, PI4K2A (By similarity).
CC       {ECO:0000250|UniProtKB:Q12768}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q12768}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q12768}. Early endosome
CC       {ECO:0000250|UniProtKB:Q12768}. Note=Colocalizes with SYP/synaptophysin
CC       in the external molecular layer of the dentate gyrus and in motoneurons
CC       of the ventral horn of spinal cord. {ECO:0000250|UniProtKB:Q12768}.
CC   -!- SIMILARITY: Belongs to the strumpellin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR860817; CAH92926.1; -; mRNA.
DR   RefSeq; NP_001126722.1; NM_001133250.2.
DR   AlphaFoldDB; Q5R5P0; -.
DR   SMR; Q5R5P0; -.
DR   STRING; 9601.ENSPPYP00000021175; -.
DR   GeneID; 100173723; -.
DR   KEGG; pon:100173723; -.
DR   CTD; 9897; -.
DR   eggNOG; KOG3666; Eukaryota.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019393; WASH_strumpellin.
DR   PANTHER; PTHR15691; PTHR15691; 1.
DR   Pfam; PF10266; Strumpellin; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Endosome; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1159
FT                   /note="WASH complex subunit 5"
FT                   /id="PRO_0000318930"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12768"
SQ   SEQUENCE   1159 AA;  134296 MW;  880A3C9E0A1018A9 CRC64;
     MLDFLAENNL CGQAILRIVS CGNAIIAELL RLSEFIPAVF RLKDRADQQK YGDIIFDFSY
     FKGPELWESK LDAKPELQDL DEEFRENNIE IVTRFYLAFQ SVHKYIVDLN RYLDDLNEGV
     YIQQTLETVL LNEDGKQLLC EALYLYGVML LVIDQKIEGE VRERMLVSYY RYSAARSSAD
     SNMDDICKLL RSTGYSSQPG ARRPPNYPES YFQRVPINES FISMVIGRLR SDDIYNQVSA
     YPLPEHRSTA LANQAAMLYV ILYFEPSILH THQAKMREIV DKYFPDNWVI SIYMGITVNL
     VDAWEPYKAA KTALNNTLDL SNVREQASRY ATVSERVHAQ VQQFLKEGYL REEMVLDNIP
     KLLNCLRDCN VAIRWLMLHT ADSACDPNNK RLRQIKDQIL TDSRYNPRIL FQLLLDTAQF
     EFILKEMFKQ MLSEKQTKWE HYKKEGSERM TELADVFSGV KPLTRVEKNE NLQAWFREIS
     KQILSLNYDD STAAGRKTVQ LIQALEEVQE FHQLESNLQV CQFLADTRKF LHQMIRTINI
     KEEVLITMQI VGDLSFAWQL IDSFTSIMQE SIRVNPSMVT KLRATFLKLA SALDLPLLRI
     NQANSPDLLS VSQYYSGELV SYVRKVLQII PESMFTSLLK IIKLQTHDII EVPTRLDKDK
     LRDYAQLGPR YEVAKLTHAI SIFTEGILMM KTTLVGIIKV DPKQLLEDGI RKELVKRVAF
     ALHRGLIFNP RAKPSELMPK LKELGATMDG FHRSFEYIQD YVNIYGLKIW QEEVSRIINY
     NVEQECNNFL RTKIQDWQSM YQSTHIPIPK FTPVDESVTF IGRLCREILR ITDPKMTCHI
     DQLNTWYDMK THQEVTSSRL FSEIQTTLGT FGLNGLDRLL CFMIVKELQN FLSMFQKIIL
     RDRTVQDTLK TLMNAVSPLK SIVANSNKIY FSAIAKTQKI WTAYLEAIMK VGQMQILRQQ
     IANELNYSCR FDSKHLAAAL ENLNKALLAD IEAHYQDPSL PYPKEDNTLL YEITAYLEAA
     GIHNPLNKIY ITTKRLPYFP IVNFLFLIAQ LPKLQYNKNL GMVCRKPTDP VDWPPLVLGL
     LTLLKQFHSR YTEQFLALIG QFICSTVEQC TSQKIPEIPA DVVGALLFLE DYARYTKLPR
     RVAEAHVPNF IFDEFRTVL