VPS53_MOUSE
ID VPS53_MOUSE Reviewed; 832 AA.
AC Q8CCB4; Q8C7U0; Q8CIA1; Q9CX82; Q9D6T7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Vacuolar protein sorting-associated protein 53 homolog;
GN Name=Vps53;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Colon, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND THR-391, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=Q8CCB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCB4-2; Sequence=VSP_016239;
CC -!- SIMILARITY: Belongs to the VPS53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK009970; BAB26620.1; ALT_INIT; mRNA.
DR EMBL; AK019408; BAB31707.1; -; mRNA.
DR EMBL; AK033495; BAC28318.1; -; mRNA.
DR EMBL; AK049259; BAC33641.1; -; mRNA.
DR EMBL; AL591129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034371; AAH34371.1; -; mRNA.
DR CCDS; CCDS25060.1; -. [Q8CCB4-1]
DR RefSeq; NP_080940.2; NM_026664.3. [Q8CCB4-1]
DR AlphaFoldDB; Q8CCB4; -.
DR SMR; Q8CCB4; -.
DR BioGRID; 212792; 11.
DR STRING; 10090.ENSMUSP00000061317; -.
DR iPTMnet; Q8CCB4; -.
DR PhosphoSitePlus; Q8CCB4; -.
DR EPD; Q8CCB4; -.
DR jPOST; Q8CCB4; -.
DR MaxQB; Q8CCB4; -.
DR PaxDb; Q8CCB4; -.
DR PeptideAtlas; Q8CCB4; -.
DR PRIDE; Q8CCB4; -.
DR ProteomicsDB; 275185; -. [Q8CCB4-1]
DR ProteomicsDB; 275186; -. [Q8CCB4-2]
DR Antibodypedia; 10256; 134 antibodies from 26 providers.
DR Ensembl; ENSMUST00000056601; ENSMUSP00000061317; ENSMUSG00000017288. [Q8CCB4-1]
DR Ensembl; ENSMUST00000108419; ENSMUSP00000104057; ENSMUSG00000017288. [Q8CCB4-2]
DR GeneID; 68299; -.
DR KEGG; mmu:68299; -.
DR UCSC; uc007kfa.1; mouse. [Q8CCB4-1]
DR UCSC; uc011xzq.1; mouse. [Q8CCB4-2]
DR CTD; 55275; -.
DR MGI; MGI:1915549; Vps53.
DR VEuPathDB; HostDB:ENSMUSG00000017288; -.
DR eggNOG; KOG2180; Eukaryota.
DR GeneTree; ENSGT00390000015165; -.
DR HOGENOM; CLU_007339_0_0_1; -.
DR InParanoid; Q8CCB4; -.
DR OMA; YKFAEAK; -.
DR OrthoDB; 1379600at2759; -.
DR PhylomeDB; Q8CCB4; -.
DR TreeFam; TF106150; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 68299; 11 hits in 71 CRISPR screens.
DR ChiTaRS; Vps53; mouse.
DR PRO; PR:Q8CCB4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CCB4; protein.
DR Bgee; ENSMUSG00000017288; Expressed in pigmented layer of retina and 255 other tissues.
DR ExpressionAtlas; Q8CCB4; baseline and differential.
DR Genevisible; Q8CCB4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; ISO:MGI.
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 1: Evidence at protein 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_0000215190"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..142
FT /evidence="ECO:0000255"
FT COMPBIAS 798..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:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VIR6"
FT VAR_SEQ 230..406
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016239"
FT CONFLICT 85
FT /note="G -> V (in Ref. 1; BAB31707)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="S -> G (in Ref. 1; BAB26620)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="D -> E (in Ref. 1; BAB26620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 94423 MW; 7B9C9FFA702EE88E CRC64;
MMEEEELEFV EELEAVLQLT PEVQLAIEQV FPSQDPLDQA DFNAVEYINT LFPTEQSLAN
IDDVVNKIRL KIRRLDDNIR TVVRGQTNVG QDGRQALEEA QKAIQQLFGK IKDIKDKAEK
SEQMVKEITR DIKQLDHAKR HLTTSITTLN HLHMLAGGVD SLEAMTRRRQ YGEVANLLQG
VMNVLEHFHK YMGIPQIRQL SERVKAAQTE LGQQILADFE EAFPSQGTKR PGGPSNVLRD
ACLVANILDP RIKQEIIKKF IKQHLSEYLV LFQENQDVAW LDKIDRRYAW VKRQLVDYEE
KYGRMFPREW CMTERISVEF CHVTRAELSK IMRARAKEIE VKLLLFAIQR TTNFEGFLAK
RFSGCTLTDG TLKKLESPPP STNPFLEDET TPEMEELALE KGELEQPKKP KAPDNPFHGI
VSKCFEPHLY VYIESQDKNL SELIDRFVAD FKAQGPPKPN TDEGGAVLPS CADLFVYYKK
CMVQCSQLST GEPMIALTTI FQKYLREYAW KILSGNLPKT SSSSGGLTIS SLLKEKEGSE
VARFTLEELC LICSILSTAE YCLATTQQLE EKLKEKVDVS LTERINLTGE MDTFSTVISS
SIQLLVQDLD AACDPALIAM SKMPWQNVEH VGDQSPYVTS VILHIKQNVP IIRDNLASTR
KYFTQFCIKF ANSFIPKFIT HLFKCKPISM VGAEQLLLDT HSLKMVLLDL PSIGSQVVRK
APASYTKIVV KGMTRAEMIL KVVMAPHEPL VVFVDNYIKL LTDCNSETFQ KILDMKGLKR
SEQSSMLELL RQRLPAPPSG TEGSSTLSLI APTPEQESSR IRKLEKLIKK RL
