VPS53_PONAB
ID VPS53_PONAB Reviewed; 832 AA.
AC Q5R5J4; A0A2J8SNJ1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Vacuolar protein sorting-associated protein 53 homolog;
GN Name=VPS53;
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] (ISOFORM 2).
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the GARP complex that is involved in
CC retrograde transport from early and late endosomes to the trans-Golgi
CC network (TGN). The GARP complex is required for the maintenance of the
CC cycling of mannose 6-phosphate receptors between the TGN and endosomes,
CC this cycling is necessary for proper lysosomal sorting of acid
CC hydrolases such as CTSD. Acts as component of the EARP complex that is
CC involved in endocytic recycling. The EARP complex associates with Rab4-
CC positive endosomes and promotes recycling of internalized transferrin
CC receptor (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q5VIR6}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, also called VFT (VPS fifty-three) complex, composed of VPS51,
CC VPS52, VPS53 and VPS54 (By similarity). Component of the endosome-
CC associated retrograde protein (EARP) complex, composed of VPS51, VPS52,
CC VPS53 and VPS50/Syndetin (By similarity). EIPR1 interacts with both
CC EARP and GARP complexes and mediates the recruitment of the GARP
CC complex to the trans-Golgi network (By similarity). Interacts with
CC VPS50 in an EIPR1-independent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q5VIR6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q5VIR6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5VIR6}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q5VIR6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5VIR6}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q5VIR6}. Note=Localizes to the trans-Golgi
CC network as part of the GARP complex, while it localizes to recycling
CC endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q5VIR6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R5J4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R5J4-2; Sequence=VSP_060666, VSP_060667;
CC -!- SIMILARITY: Belongs to the VPS53 family. {ECO:0000305}.
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DR EMBL; CR860864; CAH92972.1; -; mRNA.
DR EMBL; NDHI03003557; PNJ22341.1; -; Genomic_DNA.
DR RefSeq; NP_001126755.1; NM_001133283.1. [Q5R5J4-2]
DR AlphaFoldDB; Q5R5J4; -.
DR SMR; Q5R5J4; -.
DR STRING; 9601.ENSPPYP00000008741; -.
DR Ensembl; ENSPPYT00000009098; ENSPPYP00000008741; ENSPPYG00000007757. [Q5R5J4-1]
DR GeneID; 100173757; -.
DR KEGG; pon:100173757; -.
DR CTD; 55275; -.
DR eggNOG; KOG2180; Eukaryota.
DR GeneTree; ENSGT00390000015165; -.
DR InParanoid; Q5R5J4; -.
DR OrthoDB; 1379600at2759; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR Gene3D; 1.10.357.110; -; 1.
DR InterPro; IPR039766; Vps53.
DR InterPro; IPR038260; Vps53_C_sf.
DR InterPro; IPR007234; Vps53_N.
DR PANTHER; PTHR12820; PTHR12820; 1.
DR Pfam; PF04100; Vps53_N; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Coiled coil; Endosome; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..832
FT /note="Vacuolar protein sorting-associated protein 53
FT homolog"
FT /id="PRO_0000215191"
FT REGION 373..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 97..138
FT /evidence="ECO:0000255"
FT COMPBIAS 395..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VIR6"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VIR6"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VIR6"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VIR6"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VIR6"
FT VAR_SEQ 696..699
FT /note="LLLD -> VRWT (in isoform 2)"
FT /id="VSP_060666"
FT VAR_SEQ 700..832
FT /note="Missing (in isoform 2)"
FT /id="VSP_060667"
SQ SEQUENCE 832 AA; 94422 MW; 905BC066D21AD3CB CRC64;
MMEEEELEFV EELEAVLQLT PEVQLAIEQV FPSQDPLDRA DFNAVEYINT LFPTEQSLAN
IDEVVNKIRL KIRRLDDNIR TVVRGQTNVG QDGRQALEEA QKAIQQLFGK IKDIKDKAEK
SEQMVKEITR DIKQLDHAKR HLTTSITTLN HLHMLAGGVD SLEAMTRRRQ YGEVANLLQG
VMNVLEHFHK YMGIPQIRQL SERVKAAQTE LGQQILADFE EAFPSQGTKR PGGPSNVLRD
ACLVANILDP RIKQEIIKKF IKQHLSEYLV LFQENQDVAW LDKIDRRYAW IKRQLVDYEE
KYGRMFPREW CMAERIAVEF CHVTRTELAK IMRTRAKEIE VKLLLFAIQR TTNFEGFLAK
RFSGCTLTDG TLKKLESPPP STNPFLEDEP TPEMEELATE KGDLDQPKKP KAPDNPFHGI
VSKCFEPHLY VYIESQDKNL GELIDRFVAD FKAQGPPKPN TDEGGAVLPS CADLFVYYKK
CMVQCSQLST GEPMIALTTI FQKYLREYAW KILSGNLPKT TTSSGGLTIS SLLKEKEGSE
VAKFTLEELC LICSILSTAE YCLATTQQLE EKLKEKVDVS LIERINLTGE MDTFSTVISS
SIQLLVQDLD AACDPALTAM SKMQWQNVEH VGDQSPYVTS VILHIKQNVP IIRDNLASTR
KYFTQFCIKF ANSFIPKFIT HLFKCKPISM VGAEQLLLDT HSLKMVLLDL PSIGSQVVRK
APASYTKIVV KGMTRAEMIL KVVMAPHEPL VVFVDNYIKL LTDCNTETFQ KILDMKGLKR
SEQSSMLELL RQRLPAPPSG AESSGSLSLM APTPEQESSR IRKLEKLIKK RL
