VPS51_MOUSE
ID VPS51_MOUSE Reviewed; 782 AA.
AC Q3UVL4; Q0VF89; Q0VF90; Q3UK22; Q9CXM6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
DE AltName: Full=Protein fat-free homolog;
GN Name=Vps51; Synonyms=Ffr;
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Head, and Urinary bladder;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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
CC protein retrieval from endosomes to the TGN, acid hydrolase sorting,
CC lysosome function, endosomal cholesterol traffic and autophagy. VPS51
CC participates in retrograde transport of acid hydrolase receptors,
CC likely by promoting tethering and SNARE-dependent fusion of endosome-
CC derived carriers to the TGN. Acts as component of the EARP complex that
CC is involved in endocytic recycling. The EARP complex associates with
CC Rab4-positive endosomes and promotes recycling of internalized
CC transferrin receptor (TFRC) to the plasma membrane.
CC {ECO:0000250|UniProtKB:Q9UID3}.
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 STX6
CC (By similarity). Interacts with VPS50 and VPS54 in an EIPR1-independent
CC manner (By similarity). {ECO:0000250|UniProtKB:Q9UID3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9UID3}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9UID3}. 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:Q9UID3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UVL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UVL4-2; Sequence=VSP_036128, VSP_036129;
CC Name=3;
CC IsoId=Q3UVL4-3; Sequence=VSP_036126, VSP_036127;
CC -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI18932.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK014229; BAB29217.1; -; mRNA.
DR EMBL; AK137155; BAE23255.1; -; mRNA.
DR EMBL; AK146211; BAE26981.1; -; mRNA.
DR EMBL; AC131692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466612; EDL33203.1; -; Genomic_DNA.
DR EMBL; BC118930; AAI18931.1; -; mRNA.
DR EMBL; BC118931; AAI18932.1; ALT_FRAME; mRNA.
DR CCDS; CCDS37894.1; -. [Q3UVL4-1]
DR RefSeq; NP_001074510.1; NM_001081041.1. [Q3UVL4-1]
DR AlphaFoldDB; Q3UVL4; -.
DR BioGRID; 212892; 13.
DR IntAct; Q3UVL4; 1.
DR MINT; Q3UVL4; -.
DR STRING; 10090.ENSMUSP00000123994; -.
DR iPTMnet; Q3UVL4; -.
DR PhosphoSitePlus; Q3UVL4; -.
DR SwissPalm; Q3UVL4; -.
DR EPD; Q3UVL4; -.
DR jPOST; Q3UVL4; -.
DR MaxQB; Q3UVL4; -.
DR PaxDb; Q3UVL4; -.
DR PeptideAtlas; Q3UVL4; -.
DR PRIDE; Q3UVL4; -.
DR ProteomicsDB; 297820; -. [Q3UVL4-1]
DR ProteomicsDB; 297821; -. [Q3UVL4-2]
DR ProteomicsDB; 297822; -. [Q3UVL4-3]
DR Antibodypedia; 49945; 86 antibodies from 26 providers.
DR Ensembl; ENSMUST00000025711; ENSMUSP00000025711; ENSMUSG00000024797. [Q3UVL4-1]
DR Ensembl; ENSMUST00000160590; ENSMUSP00000123857; ENSMUSG00000024797. [Q3UVL4-3]
DR GeneID; 68505; -.
DR KEGG; mmu:68505; -.
DR UCSC; uc008ghb.1; mouse. [Q3UVL4-1]
DR UCSC; uc008ghc.1; mouse. [Q3UVL4-2]
DR UCSC; uc008ghd.1; mouse. [Q3UVL4-3]
DR CTD; 738; -.
DR MGI; MGI:1915755; Vps51.
DR VEuPathDB; HostDB:ENSMUSG00000024797; -.
DR eggNOG; KOG2346; Eukaryota.
DR GeneTree; ENSGT00390000001738; -.
DR HOGENOM; CLU_020677_0_0_1; -.
DR InParanoid; Q3UVL4; -.
DR OMA; HTIEPRT; -.
DR OrthoDB; 1305393at2759; -.
DR PhylomeDB; Q3UVL4; -.
DR TreeFam; TF314825; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 68505; 16 hits in 73 CRISPR screens.
DR ChiTaRS; Vps51; mouse.
DR PRO; PR:Q3UVL4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3UVL4; protein.
DR Bgee; ENSMUSG00000024797; Expressed in granulocyte and 191 other tissues.
DR ExpressionAtlas; Q3UVL4; baseline and differential.
DR Genevisible; Q3UVL4; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR GO; GO:0000938; C:GARP complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0048854; P:brain morphogenesis; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR014812; Vps51.
DR PANTHER; PTHR15954; PTHR15954; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endosome; Golgi apparatus;
KW Lipid transport; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UID3"
FT CHAIN 2..782
FT /note="Vacuolar protein sorting-associated protein 51
FT homolog"
FT /id="PRO_0000358913"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..148
FT /evidence="ECO:0000255"
FT COILED 270..292
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID3"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID3"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID3"
FT VAR_SEQ 120..140
FT /note="DTIRKMKNDFRKMEDEMDRLA -> GDPTGTHSSVLHHPHQVLTPC (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036126"
FT VAR_SEQ 141..782
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036127"
FT VAR_SEQ 482..577
FT /note="GEFCSQGVREGLIVGFIRSMCQTAQSFCDSPGEKGGATPPALLLLLSRLCLD
FT YETATISYILTLTDEQFLVQDQSPVTPVSTLCAEARETARRLLT -> VCCPLALLIRS
FT ADWPSSSLLLVFGEPWDMSPAPHNTVSSTLRVESHSQEAVWRRKCYAAGLKLEGYQGPH
FT CCQPYHRGSEAGWGGLWRRVKAKREE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036128"
FT VAR_SEQ 578..782
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036129"
FT CONFLICT 265
FT /note="A -> P (in Ref. 1; BAE26981)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> D (in Ref. 1; BAE23255)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="H -> R (in Ref. 1; BAE26981)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="L -> M (in Ref. 1; BAE26981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 86187 MW; 377198219AAF5F6C CRC64;
MAAAAAVGPG LGSGPGDSPE GPEADAPERR RKAHGMLKLY YGLSEGEVAG HPAGPDPLDP
TDLNGAHFDP EVYLDKLRRE CPLAQLMDSE TDMVRQIRAL DSDMQTLVYE NYNKFISATD
TIRKMKNDFR KMEDEMDRLA TNMAVITNFS ARISATLQDR HERITKLAGV HALLRKLQFL
FELPSRLTKC VELGAYGQAV RYQGRARAVL QQYQHLPSFR AIQDDCQVIT ARLAQQLRQR
FREGCSGAPE QAECVELLLA LGEPAEELCE EFLAHARGRL EEELSSLEAE LGPSPPAPDV
LEFTDRGGNG FVGGLCQVAA AYQELFAAQG PAGAEKLAAF AQELGGRYFA LVERRLAQEQ
GGSDNSLLVR ALDRFHRRLR APGALLAAAG LSESATEIVE RVARERLSHH LQGLKAAFLS
SLTDVRQALA APRLAGKEGP SLAELLANVA SSILSHIKTS LASVHLFTAK EVSFSNKPYF
RGEFCSQGVR EGLIVGFIRS MCQTAQSFCD SPGEKGGATP PALLLLLSRL CLDYETATIS
YILTLTDEQF LVQDQSPVTP VSTLCAEARE TARRLLTHYV KVQGLVISQM LRKSVETRDW
LSTLEPRNVR AVMKRVVEDT TAIDVQVGLL YEEGVRKAQS SDSSKRTFSV YSSSRQQGRY
APSYTPSAPM DTNLLSNIQK LFSERIDVFS PVEFNKVSVL TGIIKISLKT LLECVRLRTF
GRFGLQQVQV DCHFLQLYLW RFVADEELVH LLLDEVVASA ALRCPDPVPM EPSVVEVICE
RG
