ID   VPS41_CAEBR             Reviewed;         898 AA.
AC   Q618H8; A8XKD7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Vacuolar protein sorting-associated protein 41 homolog;
GN   Name=vps-41 {ECO:0000250|UniProtKB:Q19954}; ORFNames=CBG14653;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC       lysosomal compartments including the endocytic membrane transport
CC       pathways. Believed to act in part as a core component of the putative
CC       HOPS endosomal tethering complex which is proposed to be involved in
CC       the rab-5-to-rab-7 endosome conversion probably implicating sand-1, and
CC       via binding SNAREs and SNARE complexes to mediate tethering and docking
CC       events during SNARE-mediated membrane fusion. The HOPS complex is
CC       proposed to be recruited to rab-7 on the late endosomal membrane and to
CC       regulate late endocytic, phagocytic and autophagic traffic towards
CC       lysosomes. Within the HOPS complex, contributes to the normal
CC       development of gut granules in the adult intestine. May mediate the
CC       tethering of autophagosomes with lysosomes. Has a role in the negative
CC       regulation of apoptosis. Required for uptake of exogenous dsRNA which
CC       is used in experimental RNA silencing. {ECO:0000250|UniProtKB:P49754,
CC       ECO:0000250|UniProtKB:Q19954}.
CC   -!- SUBUNIT: Probable component of the homotypic fusion and vacuole protein
CC       sorting (HOPS) complex consisting of the core class C Vps proteins vps-
CC       11, vps-16, vps-18, and which further associates with vps-33.1, vps-39
CC       and vps-41. {ECO:0000250|UniProtKB:P49754}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:P49754}.
CC       Late endosome {ECO:0000250|UniProtKB:P49754}. Lysosome
CC       {ECO:0000250|UniProtKB:P49754}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:P49754}. Early endosome
CC       {ECO:0000250|UniProtKB:P49754}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle {ECO:0000250|UniProtKB:P49754}.
CC   -!- SIMILARITY: Belongs to the VPS41 family. {ECO:0000255}.
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DR   EMBL; HE600983; CAP33111.3; -; Genomic_DNA.
DR   RefSeq; XP_002644672.1; XM_002644626.1.
DR   AlphaFoldDB; Q618H8; -.
DR   STRING; 6238.CBG14653; -.
DR   GeneID; 8586668; -.
DR   KEGG; cbr:CBG_14653; -.
DR   CTD; 8586668; -.
DR   WormBase; CBG14653; CBP39412; WBGene00035081; Cbr-vps-41.
DR   eggNOG; KOG2066; Eukaryota.
DR   HOGENOM; CLU_001285_2_2_1; -.
DR   InParanoid; Q618H8; -.
DR   OMA; KFKYQRI; -.
DR   OrthoDB; 722805at2759; -.
DR   Proteomes; UP000008549; Chromosome X.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
DR   GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   GO; GO:0006624; P:vacuolar protein processing; ISS:UniProtKB.
DR   GO; GO:0007034; P:vacuolar transport; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR016902; VPS41.
DR   InterPro; IPR045111; Vps41/Vps8.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR12616; PTHR12616; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   PIRSF; PIRSF028921; VPS41; 1.
DR   SMART; SM00299; CLH; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Cytoplasmic vesicle; Endosome; Golgi apparatus; Lysosome;
KW   Membrane; Metal-binding; Protein transport; Reference proteome; Transport;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..898
FT                   /note="Vacuolar protein sorting-associated protein 41
FT                   homolog"
FT                   /id="PRO_0000298663"
FT   REPEAT          614..756
FT                   /note="CHCR"
FT   ZN_FING         835..890
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  102403 MW;  35E3C03A741E0EC8 CRC64;
     MDESNDKENE FGDSFLEDSG DITRTTEDED EAPLEPRFKY ERLEGESTLP FMKTATFTSI
     DLHDKFIAIG TASGLIYILD HHGYGNFDSV PPLKPHRCAV SKLKFDETGS YILSCANDSK
     LVVSGIGNDK LCCTVNIQVM PKSICFSPDF IRQQSGHCFI MGERNLVLYE KRLFQYKASN
     LYSGSERDGF IHCCSWNDNL IAFTNDTGTR VYERGTEKIL TSVQPTHDVD RVRSSRCPPK
     HMWMSENTLV IGWADTVTVL KIKGNEGMRK GEIHHIFHVS MFISGISYLP KNGSDYELFL
     VGLQMEGEDF DDCASVMSTM TTLTAMESSA TATLKTCVIR PLGLKDYELQ SEDEIVNIRL
     STHTLPYMIH GLGIPYLSTY FILTTKQIIM AVPYGPEDGI KWRLQYKLYT EAFEMAKEHA
     DMLAKTDVSP KKVGRKIIEG YLESKKARVA ASWLSSICGD CKEEWEWAVD RFHDAKMSTL
     LGDVLPDSKP RLDPSAYEKV LLASLFNNVK LFRRLVQTWS PDLYMTSTII DQTQWRIQQI
     SKSEDIEDVE EVEKILMDAL AHLYLYERKY ESALKILMIC QDFQIFNVID KHQLFDLVKD
     QISDLMNINS ERALRLLLDN ADSVEPSFVM AKINGQPKLQ LAYLTKLMSR NEGIEFADKA
     VQLYADHEKK KLLPFLKKNV NYNVTKARKL CSDRGFVEET IFLLAKSGNH YEAVKMMVRE
     YKNIEKVIAY CKDQNDRDLW IHLLEVVADF PTHFSQLIIE ASNCLDPILI MDKLPDDVDI
     PNLSEALEKL LTDFTNYVEL QQCCYDSTLN DLHVLTNNLM LASDKSVSVS LMTRCSLCSQ
     VIMNTGQDMI PRKFNDIKVF KCGHIFHLTC SASEIDRRQM IEDGICIACS DNSDHVNV