VPS8_MOUSE
ID VPS8_MOUSE Reviewed; 1427 AA.
AC Q0P5W1; Q3UR93; Q80TR5; Q8K280;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Vacuolar protein sorting-associated protein 8 homolog;
GN Name=Vps8; Synonyms=Kiaa0804;
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 3).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 485-1427 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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, Kidney, Lung, and Spleen;
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).
RN [5]
RP INTERACTION WITH RAB5C, AND SUBUNIT.
RX PubMed=25266290; DOI=10.1111/tra.12232;
RA Perini E.D., Schaefer R., Stoeter M., Kalaidzidis Y., Zerial M.;
RT "Mammalian CORVET is required for fusion and conversion of distinct early
RT endosome subpopulations.";
RL Traffic 15:1366-1389(2014).
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking of the
CC endocytic membrane transport pathway. Believed to act as a component of
CC the putative CORVET endosomal tethering complexes which is proposed to
CC be involved in the Rab5-to-Rab7 endosome conversion probably
CC implicating MON1A/B, and via binding SNAREs and SNARE complexes to
CC mediate tethering and docking events during SNARE-mediated membrane
CC fusion. The CORVET complex is proposed to function as a Rab5 effector
CC to mediate early endosome fusion probably in specific endosome
CC subpopulations. Functions predominantly in APPL1-containing endosomes
CC (By similarity). {ECO:0000250|UniProtKB:Q8N3P4}.
CC -!- SUBUNIT: Interacts with RAB5C (PubMed:25266290). Interacts with
CC TGFBRAP1 (By similarity). Component of the putative class C core
CC vacuole/endosome tethering (CORVET) complex; the core of which is
CC composed of the class C Vps proteins VPS11, VPS16, VPS18 and VPS33A,
CC associated with VPS8 and TGFBRAP1 (PubMed:25266290).
CC {ECO:0000250|UniProtKB:Q8N3P4, ECO:0000269|PubMed:25266290,
CC ECO:0000305|PubMed:25266290}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0P5W1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0P5W1-2; Sequence=VSP_023254, VSP_023255;
CC Name=3;
CC IsoId=Q0P5W1-3; Sequence=VSP_023252, VSP_023253;
CC -!- SIMILARITY: Belongs to the VPS8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32214.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC26237.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122375; BAC65657.1; ALT_INIT; mRNA.
DR EMBL; AK029007; BAC26237.1; ALT_FRAME; mRNA.
DR EMBL; AK141678; BAE24795.1; -; mRNA.
DR EMBL; BC032214; AAH32214.1; ALT_INIT; mRNA.
DR EMBL; BC055323; AAH55323.1; -; mRNA.
DR CCDS; CCDS70700.1; -. [Q0P5W1-3]
DR CCDS; CCDS70701.1; -. [Q0P5W1-1]
DR RefSeq; NP_001272822.1; NM_001285893.1. [Q0P5W1-1]
DR RefSeq; NP_001272823.1; NM_001285894.1. [Q0P5W1-3]
DR AlphaFoldDB; Q0P5W1; -.
DR SMR; Q0P5W1; -.
DR BioGRID; 229039; 5.
DR IntAct; Q0P5W1; 1.
DR STRING; 10090.ENSMUSP00000093905; -.
DR iPTMnet; Q0P5W1; -.
DR PhosphoSitePlus; Q0P5W1; -.
DR MaxQB; Q0P5W1; -.
DR PaxDb; Q0P5W1; -.
DR PeptideAtlas; Q0P5W1; -.
DR PRIDE; Q0P5W1; -.
DR ProteomicsDB; 297586; -. [Q0P5W1-1]
DR ProteomicsDB; 297587; -. [Q0P5W1-2]
DR ProteomicsDB; 297588; -. [Q0P5W1-3]
DR Antibodypedia; 33827; 79 antibodies from 21 providers.
DR DNASU; 209018; -.
DR Ensembl; ENSMUST00000096191; ENSMUSP00000093905; ENSMUSG00000033653. [Q0P5W1-2]
DR Ensembl; ENSMUST00000117598; ENSMUSP00000112937; ENSMUSG00000033653. [Q0P5W1-1]
DR Ensembl; ENSMUST00000118923; ENSMUSP00000112636; ENSMUSG00000033653. [Q0P5W1-3]
DR GeneID; 209018; -.
DR KEGG; mmu:209018; -.
DR UCSC; uc007yrj.2; mouse. [Q0P5W1-1]
DR UCSC; uc012adi.2; mouse. [Q0P5W1-3]
DR CTD; 23355; -.
DR MGI; MGI:2146407; Vps8.
DR VEuPathDB; HostDB:ENSMUSG00000033653; -.
DR eggNOG; KOG2079; Eukaryota.
DR GeneTree; ENSGT00390000010672; -.
DR HOGENOM; CLU_000917_1_2_1; -.
DR InParanoid; Q0P5W1; -.
DR OMA; WAHQDKH; -.
DR TreeFam; TF314244; -.
DR BioGRID-ORCS; 209018; 2 hits in 67 CRISPR screens.
DR ChiTaRS; Vps8; mouse.
DR PRO; PR:Q0P5W1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q0P5W1; protein.
DR Bgee; ENSMUSG00000033653; Expressed in proximal tubule and 224 other tissues.
DR ExpressionAtlas; Q0P5W1; baseline and differential.
DR Genevisible; Q0P5W1; MM.
DR GO; GO:0033263; C:CORVET complex; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034058; P:endosomal vesicle fusion; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025941; Vps8_central_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12816; Vps8; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Phosphoprotein; Reference proteome;
KW WD repeat; Zinc; Zinc-finger.
FT CHAIN 1..1427
FT /note="Vacuolar protein sorting-associated protein 8
FT homolog"
FT /id="PRO_0000278268"
FT REPEAT 193..234
FT /note="WD"
FT ZN_FING 1257..1309
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1311..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3P4"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3P4"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3P4"
FT VAR_SEQ 178
FT /note="F -> FGK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023252"
FT VAR_SEQ 965..994
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023253"
FT VAR_SEQ 1278..1292
FT /note="SCGHLYHSFCLQSKE -> RFLYWVTGASPIQPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023254"
FT VAR_SEQ 1293..1427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023255"
FT CONFLICT 591
FT /note="R -> G (in Ref. 2; BAC26237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1427 AA; 161146 MW; 7E88538003B36B72 CRC64;
METEPDQEHL DQNPCARTVE EELSKSFNLE ASLSKFSCLD LDKELEFRSD LIDDKEFDIP
QVDTPPTLES ILNETDDEDE SFVLEDPTLL NVDTIDSHSY DTSSVASSDS GDRANLKRKK
KLPDSFSLHG SVMRHSLLKG ISAQIVSAAD KVDAGLPTAI AVSSLIAVGT SHGLALIFDQ
NQALRLCLGS TSVGGQYGAI SALSINNDCS RLLCGFAKGQ ITMWDLASGK LLRSITDAHP
PGTAILHIKF TDDPTLAICN DSGGSVFELT FKRVMGVRTC ESRCLFSGSK GEVCCIEPLH
SKPELKDHPI TQFSLLAMAS LTKILVIGLK PSLKVWMTFP YGRMDPSSVP LLAWHFVAVN
NSVNPMLAFC RGDMVHFLLV KRDESGAIHV TKQKHLHLYY DLINFTWINS RTVVLLDSVE
KLHVIDRQTQ EELETMEISE VQLVYNSSHF KSLATGGNVS QALALVGEKA CYQSISSYGG
QIFYLGTKSV YVMMLRSWRE RMDHLLKQDC LTEALALAWS FHEGKAKAVV GLSGDVSKRK
AVVADRMVEI LFHYADRALK KCPDQGKIQV MEQHFQDTVP VIVDYCLLLQ RKDLLFGQMY
DKLSENSVAK GVFLECLEPY ILSDKLVGIT PQVMKDLIVH FQDKKLLENV EALIVHMDIT
SLDIQQVVLM CWENRLYDAM VYVYNRGMNE FISPMEKLFK VIAPPLNAGK TLTDEQVVMG
NKLLVYISCC LAGRAYPLGD IPEDLVPLVK NQVFEFLIRL HSVEASSEEE VYPYVRTLLH
FDTREFLNVL ALTFEDFKND KQAVEYQQRI VDILLKVMVE NSDFTPSQVG CLFTFLARQL
AKPDNTLFVN RTLFDQVLEF LCSPDDDSRH SERQQVLLEL LQAGGIVQFE ESRLIRMAEK
AEFYQICEFM YEREHQYDKI IDCYLHDPLR EEEVFNYIHN ILSIPGHSAE EKQSVWQKAM
NHMEELVSLK PCKAAELVAT HFSEQIEVVI GQLQNQLLLF KFLRSLLDPR EGVHVNQELL
QIPPHITEQF IELLCQFSPD QVIQTLQVLE CYRLEETIQI TQKYQLHEVT AYLLEKKGDA
HGAFLLLLER LQSRLQEMTR QDENTKEDIL LKGVEDTMVE TIALCQRNSQ NLNQQQREAL
WFPLLEAMMT PQKLSSSAAA PHPHCEALKS LTMQVLNSMA AFIALPSILQ RILQDPIYGK
GKLGEIQGLI LGMLDTFNYE QTLLETTASL LNQDLHWSLC NLRASVSRGL NPKQDYCSIC
LQQYKRRQEM ADEIIVFSCG HLYHSFCLQS KECTLEVEGQ TRWACHKCSS SNKAGKLSEN
PSENKKGRIT SSQVKMSPSY HQSKGDPPAR KANSEPVLDP QQMQAFDQLC RLYRGSSRLA
LLTELSQNRG GDSCRPFAGP QSGPAFNSVF QKENFQLQLA PPPVAED
