VPS35_BOVIN
ID VPS35_BOVIN Reviewed; 796 AA.
AC Q2HJG5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Vacuolar protein sorting-associated protein 35;
DE AltName: Full=Vesicle protein sorting 35;
GN Name=VPS35;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC (CSC). The CSC is believed to be the core functional component of
CC retromer or respective retromer complex variants acting to prevent
CC missorting of selected transmembrane cargo proteins into the lysosomal
CC degradation pathway. The recruitment of the CSC to the endosomal
CC membrane involves RAB7A and SNX3. The CSC seems to associate with the
CC cytoplasmic domain of cargo proteins predominantly via VPS35; however,
CC these interactions seem to be of low affinity and retromer SNX proteins
CC may also contribute to cargo selectivity thus questioning the classical
CC function of the CSC. The SNX-BAR retromer mediates retrograde transport
CC of cargo proteins from endosomes to the trans-Golgi network (TGN) and
CC is involved in endosome-to-plasma membrane transport for cargo protein
CC recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN
CC transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-
CC retromer is believed to be involved in endosome-to-plasma membrane
CC trafficking and recycling of a broad spectrum of cargo proteins. The
CC CSC seems to act as recruitment hub for other proteins, such as the
CC WASH complex and TBC1D5. Required for retrograde transport of lysosomal
CC enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of
CC the polymeric immunoglobulin receptor (pIgR-pIgA). Required for
CC endosomal localization of WASHC2. Mediates the association of the CSC
CC with the WASH complex via WASHC2. Required for the endosomal
CC localization of TBC1D5 (By similarity). {ECO:0000250|UniProtKB:Q96QK1}.
CC -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC complex (CSC), also described as vacuolar protein sorting subcomplex
CC (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35. The CSC has
CC a highly elongated structure with VPS26 and VPS29 binding independently
CC at opposite distal ends of VPS35 as central platform. The CSC is
CC believed to associate with variable sorting nexins to form functionally
CC distinct retromer complex variants. The originally described retromer
CC complex (also called SNX-BAR retromer) is a pentamer containing the CSC
CC and a heterodimeric membrane-deforming subcomplex formed between SNX1
CC or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the affinity
CC between the respective CSC and SNX-BAR subcomplexes is low. The CSC
CC associates with SNX3 to form a SNX3-retromer complex. The CSC
CC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to
CC form the SNX27-retromer complex. Interacts with VPS26A, VPS29, VPS26B
CC and LRRK2 (By similarity). Interacts with SNX1, SNX2, IGF2R, SNX3,
CC GOLPH3, SLC11A2, WASHC2, FKBP15, WASHC1, EHD1. Interacts with MAGEL2;
CC leading to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase complex
CC retromer-containing endosomes (By similarity). Interacts with SORCS2
CC (By similarity). {ECO:0000250|UniProtKB:Q96QK1,
CC ECO:0000250|UniProtKB:Q9EQH3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC Endosome {ECO:0000250|UniProtKB:Q96QK1}. Early endosome {ECO:0000305}.
CC Late endosome {ECO:0000305}. Note=Localizes to tubular profiles
CC adjacent to endosomes. {ECO:0000250|UniProtKB:Q96QK1}.
CC -!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
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DR EMBL; BC105430; AAI05431.1; -; mRNA.
DR RefSeq; NP_001039723.1; NM_001046258.1.
DR AlphaFoldDB; Q2HJG5; -.
DR SMR; Q2HJG5; -.
DR STRING; 9913.ENSBTAP00000003239; -.
DR PaxDb; Q2HJG5; -.
DR PeptideAtlas; Q2HJG5; -.
DR PRIDE; Q2HJG5; -.
DR Ensembl; ENSBTAT00000003239; ENSBTAP00000003239; ENSBTAG00000002493.
DR GeneID; 521864; -.
DR KEGG; bta:521864; -.
DR CTD; 55737; -.
DR VEuPathDB; HostDB:ENSBTAG00000002493; -.
DR VGNC; VGNC:36818; VPS35.
DR eggNOG; KOG1107; Eukaryota.
DR GeneTree; ENSGT00390000007315; -.
DR HOGENOM; CLU_005836_1_0_1; -.
DR InParanoid; Q2HJG5; -.
DR OMA; WWVVENP; -.
DR OrthoDB; 316875at2759; -.
DR TreeFam; TF105659; -.
DR Reactome; R-BTA-3238698; WNT ligand biogenesis and trafficking.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000002493; Expressed in milk and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0099073; C:mitochondrion-derived vesicle; IEA:Ensembl.
DR GO; GO:0030904; C:retromer complex; ISS:UniProtKB.
DR GO; GO:0030906; C:retromer, cargo-selective complex; IEA:Ensembl.
DR GO; GO:0097422; C:tubular endosome; ISS:UniProtKB.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0099074; P:mitochondrion to lysosome transport; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1902823; P:negative regulation of late endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; IEA:Ensembl.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:Ensembl.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:2000331; P:regulation of terminal button organization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB.
DR Gene3D; 1.25.40.660; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005378; Vps35.
DR InterPro; IPR042491; Vps35_C.
DR PANTHER; PTHR11099; PTHR11099; 1.
DR Pfam; PF03635; Vps35; 1.
DR PIRSF; PIRSF009375; Retromer_Vps35; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..796
FT /note="Vacuolar protein sorting-associated protein 35"
FT /id="PRO_0000253039"
FT REGION 25..44
FT /note="Interaction with SNX3"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 205..215
FT /note="Interaction with SNX3"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 438..796
FT /note="Interaction with SLC11A2"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 500..693
FT /note="Interaction with IGF2R cytoplasmic domain"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQH3"
FT MOD_RES 791
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQH3"
SQ SEQUENCE 796 AA; 91751 MW; 38D2AB5998CB8E69 CRC64;
MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP
KSYYELYMAI SDELHYLEVY LTDEFAKGRK VADLYELVQY AGNIIPRLYL LITVGVVYVK
SFPQSRKDIL KDLVEMCRGV QHPLRGLFLR NYLLQCTRNI LPDEGEPTDE ETTGDISDSM
DFVLLNFAEM NKLWVRMQHQ GHSRDREKRE RERQELRILV GTNLVRLSQL EGVNVERYKQ
IVLTGILEQV VNCRDALAQE YLMECIIQVF PDEFHLQTLN PFLRACAELH QNVNVKNIII
ALIDRLALFA HREDGPGIPT DIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL QVSLINLAMK
CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR LLKIPVDTYN NILTVLKLKH
FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE IVSQDQVDSI MNLVSTLIQD QPDQPVEEPD
PEDFADEQSL VGRFIHLLRS EDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA
FRYKENSKVD DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE
TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR TQCALAASKL
LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL KKALKIANQC MDPSLQVQLF
IEILNRYIYF YEKENDAVTI QVLNQLIQKI REDLPNLESS EETEQINKHF HNTLEHLRLR
RESPESEGPI YEGLIL
