VPS52_MOUSE
ID VPS52_MOUSE Reviewed; 723 AA.
AC Q8C754; Q6P4N7; Q8BQ15; Q9QWT6; Q9QWV2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Vacuolar protein sorting-associated protein 52 homolog;
GN Name=Vps52;
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=Lung;
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=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pituitary;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, 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:Q8N1B4}.
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. Component of the endosome-associated retrograde
CC protein (EARP) complex, composed of VPS51, VPS52, VPS53 and
CC VPS50/Syndetin. EIPR1 interacts with both EARP and GARP complexes and
CC mediates the recruitment of the GARP complex to the trans-Golgi
CC network. Interacts with RAB6A and STX10. Interacts with UHRF1BP1L.
CC {ECO:0000250|UniProtKB:Q8N1B4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8N1B4}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8N1B4}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q8N1B4}. 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:Q8N1B4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C754-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C754-2; Sequence=VSP_016234, VSP_016235;
CC -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC69899.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC97979.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK051732; BAC34741.1; -; mRNA.
DR EMBL; AK052523; BAC35024.1; -; mRNA.
DR EMBL; AF100956; AAC69899.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF110520; AAC97979.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC063329; AAH63329.1; -; mRNA.
DR CCDS; CCDS37574.1; -. [Q8C754-1]
DR RefSeq; NP_766208.2; NM_172620.3. [Q8C754-1]
DR AlphaFoldDB; Q8C754; -.
DR BioGRID; 230307; 8.
DR STRING; 10090.ENSMUSP00000025178; -.
DR iPTMnet; Q8C754; -.
DR PhosphoSitePlus; Q8C754; -.
DR EPD; Q8C754; -.
DR MaxQB; Q8C754; -.
DR PaxDb; Q8C754; -.
DR PeptideAtlas; Q8C754; -.
DR PRIDE; Q8C754; -.
DR ProteomicsDB; 297823; -. [Q8C754-1]
DR ProteomicsDB; 297824; -. [Q8C754-2]
DR Antibodypedia; 28991; 134 antibodies from 22 providers.
DR DNASU; 224705; -.
DR Ensembl; ENSMUST00000025178; ENSMUSP00000025178; ENSMUSG00000024319. [Q8C754-1]
DR GeneID; 224705; -.
DR KEGG; mmu:224705; -.
DR UCSC; uc008cam.1; mouse. [Q8C754-1]
DR CTD; 6293; -.
DR MGI; MGI:1330304; Vps52.
DR VEuPathDB; HostDB:ENSMUSG00000024319; -.
DR eggNOG; KOG1961; Eukaryota.
DR GeneTree; ENSGT00390000008815; -.
DR HOGENOM; CLU_010797_0_0_1; -.
DR InParanoid; Q8C754; -.
DR OMA; IHVVMVE; -.
DR OrthoDB; 158568at2759; -.
DR PhylomeDB; Q8C754; -.
DR TreeFam; TF314937; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 224705; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Vps52; mouse.
DR PRO; PR:Q8C754; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8C754; protein.
DR Bgee; ENSMUSG00000024319; Expressed in granulocyte and 199 other tissues.
DR ExpressionAtlas; Q8C754; baseline and differential.
DR Genevisible; Q8C754; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
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:0016020; C:membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0010668; P:ectodermal cell differentiation; IMP:MGI.
DR GO; GO:0048611; P:embryonic ectodermal digestive tract development; IMP:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR007258; Vps52.
DR PANTHER; PTHR14190; PTHR14190; 1.
DR Pfam; PF04129; Vps52; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N1B4"
FT CHAIN 2..723
FT /note="Vacuolar protein sorting-associated protein 52
FT homolog"
FT /id="PRO_0000213316"
FT COILED 107..127
FT /evidence="ECO:0000255"
FT COILED 194..214
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1B4"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1B4"
FT VAR_SEQ 124..191
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016234"
FT VAR_SEQ 681..715
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016235"
FT CONFLICT 458
FT /note="A -> G (in Ref. 3; AAH63329)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="N -> K (in Ref. 1; BAC34741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 82044 MW; 5209C84FCA84DF75 CRC64;
MAAAATMAAA ARELVLRAGA SDVEEEEGPL GGGSGLQEPL QLGELDITSD EFILDEVDVH
IQANLEDELV KEALKTGVDL RHYSKQVELE LQQIEQKSIR DYIQESENIA SLHNQITACD
AVLERMEQML GAFQSDLSSI SSEIRTLQEQ SGAMNIRLRN RQAVRGKLGE LVDGLVVPSA
LVTAILEAPV TEPRFLEQLQ ELDAKAAAVR EQEAMGTAAC ADVRGVLDRL RVKAVTKIRE
FILQKIYSFR KPMTNYQIPQ AALLKYRFFY QFLLGNERAT AKEIRDEYVE TLSKIYLSYY
RSYVGRLMKV QYEEVAEKDD LMGVEDTAKK GFFSKPSLRS RNTIFTLGTR GTVISPAELE
APILVPHTAQ RGEQRYPFEA LFRSQHYALL DNSCREYLFI CEFFIVSGPA AHDLFHAVMG
RTLSMTLKHL ESYLADCYDA IAVFLCIHIV LRFRNIAAKR DVPALDRYWE QVLALLWPRF
ELILEMNVQS VRSTDPQRLG GLDTRPHYIT RRYAEFSSAL VSINQTIPNE RTLQLLGQLQ
VEVENFVLRV AAEFSSRKEQ LVFLINNYDM MLGVLMERAA DDSKEVESFQ QLLNARTQEF
IEELLSPPFG GLVAFVKEAE ALIERGQAER LRGEEARVTQ LIRGFGSSWK ASVESLSQDV
MRSFTNFRNG TSIIQGALTQ LIQLYHRFHR VLSQPQLRAL PARAELINIH HLMVELKKHK
PNF
