VMS1_CAEEL
ID VMS1_CAEEL Reviewed; 618 AA.
AC P34511;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein vms-1;
GN Name=vms-1; ORFNames=K06H7.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21070972; DOI=10.1016/j.molcel.2010.10.021;
RA Heo J.M., Livnat-Levanon N., Taylor E.B., Jones K.T., Dephoure N., Ring J.,
RA Xie J., Brodsky J.L., Madeo F., Gygi S.P., Ashrafi K., Glickman M.H.,
RA Rutter J.;
RT "A stress-responsive system for mitochondrial protein degradation.";
RL Mol. Cell 40:465-480(2010).
CC -!- FUNCTION: Involved in the endoplasmic reticulum (ER)-associated
CC degradation (ERAD) pathway. Component of an evolutionarily conserved
CC system for ubiquitin-mediated mitochondria-associated protein
CC degradation (MAD) (By similarity). Dispensable for viability and growth
CC but is required for protection against oxidative stress and for wild-
CC type life span. {ECO:0000250, ECO:0000269|PubMed:21070972}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21070972}.
CC Mitochondrion {ECO:0000269|PubMed:21070972}. Note=translocates from the
CC cytosol to mitochondria upon exposure to hydrogen peroxide.
CC -!- TISSUE SPECIFICITY: In larval stages and in adults, expressed in
CC intestinal cells, specific neurons in the head and the tail, and in the
CC ventral nerve cord. {ECO:0000269|PubMed:21070972}.
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
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DR EMBL; FO080533; CCD64453.1; -; Genomic_DNA.
DR PIR; S44843; S44843.
DR RefSeq; NP_498765.1; NM_066364.5.
DR AlphaFoldDB; P34511; -.
DR SMR; P34511; -.
DR BioGRID; 41347; 1.
DR IntAct; P34511; 1.
DR STRING; 6239.K06H7.3.2; -.
DR EPD; P34511; -.
DR PaxDb; P34511; -.
DR PeptideAtlas; P34511; -.
DR PRIDE; P34511; -.
DR EnsemblMetazoa; K06H7.3.1; K06H7.3.1; WBGene00019457.
DR GeneID; 176141; -.
DR KEGG; cel:CELE_K06H7.3; -.
DR UCSC; K06H7.3.1; c. elegans.
DR CTD; 176141; -.
DR WormBase; K06H7.3; CE26941; WBGene00019457; vms-1.
DR eggNOG; KOG2505; Eukaryota.
DR GeneTree; ENSGT00390000005911; -.
DR HOGENOM; CLU_014293_0_1_1; -.
DR InParanoid; P34511; -.
DR OMA; MLEWKMR; -.
DR OrthoDB; 1495271at2759; -.
DR PhylomeDB; P34511; -.
DR PRO; PR:P34511; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019457; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR041540; VATC.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF18826; bVLRF1; 1.
DR Pfam; PF18716; VATC; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Coiled coil; Cytoplasm; Metal-binding; Mitochondrion;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..618
FT /note="Protein vms-1"
FT /id="PRO_0000065404"
FT REPEAT 437..466
FT /note="ANK 1"
FT REPEAT 470..496
FT /note="ANK 2"
FT ZN_FING 59..85
FT /note="C2H2-type"
FT REGION 502..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 510..557
FT /evidence="ECO:0000255"
FT COMPBIAS 505..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 71320 MW; DE6A695E14F6EAE4 CRC64;
MGFTLKSLEF LQGVEPFRID ENHENEGASE EEEVLISAET DAGMSLMLEW KMRLSEDSDQ
CTTCNCPVDF GDRAVLLEHY QSLFHRTNTL RKARNMTVYT EEDFEGIENS ENDLTSSQTT
IGLESDDEEF DALLLPANRS FFIKNGSVFS VPRNILHVGE RDVSSVTFLR PFDCAIFLWN
GGHFAAAMFE NDKMTVQKSF HRYVARAKQG GVQSQHDSGG KGAAKSAGAQ LRRYNEQKMK
EEIQSIMSSW KSRLQKTPLL FIRCAAYHRN IFFEADAGIE TRDDRIRTIP FETKRPNIDE
ISDCWQRLQQ VSEHGAESDF RAEMLEVREK RKKLARKVAG KKRKDGGMQM ICEWSDDDEN
EDISKEKKTH HIKVRTIKKP EETVVQWPRL DDEWRQKTYN YVRQDSVEAL KEHLASLNED
VTSEANDYLR NAKIPPNRST FLHVSAANDA RKCLKYFLEE VNCDSSTKDG AGLPPYSSSA
NSDVKSIFID YRVKNETAGN WARTHIPEPK KKVELTEEQE REQAERKKEK KARQKEKEKL
KKEIAKRDVE EMEERQKYVN MSEREKRALA VDRRLAGLPP ILRCHQCGVQ LPPTPFQYSH
YNFCSTSCVA EHRKANPQ
