ID G3Q9K7_GASAC Unreviewed; 925 AA.
AC G3Q9K7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Vacuolar protein sorting-associated protein 11 homolog {ECO:0000256|PIRNR:PIRNR007860};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000026572.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000026572.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000026572.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport and
CC autophagic pathways. Believed to act as a core component of the
CC putative HOPS and CORVET endosomal tethering complexes.
CC {ECO:0000256|PIRNR:PIRNR007860}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000256|PIRNR:PIRNR007860}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR007860}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR007860}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004630, ECO:0000256|PIRNR:PIRNR007860};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630,
CC ECO:0000256|PIRNR:PIRNR007860}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004630, ECO:0000256|PIRNR:PIRNR007860}.
CC Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR007860}. Early endosome
CC {ECO:0000256|PIRNR:PIRNR007860}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000256|PIRNR:PIRNR007860}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000256|PIRNR:PIRNR007860}.
CC -!- SIMILARITY: Belongs to the VPS11 family.
CC {ECO:0000256|ARBA:ARBA00007070, ECO:0000256|PIRNR:PIRNR007860}.
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DR AlphaFoldDB; G3Q9K7; -.
DR STRING; 69293.ENSGACP00000026572; -.
DR Ensembl; ENSGACT00000026623.1; ENSGACP00000026572.1; ENSGACG00000020112.1.
DR eggNOG; KOG2114; Eukaryota.
DR GeneTree; ENSGT00940000153635; -.
DR InParanoid; G3Q9K7; -.
DR OMA; ENECPAC; -.
DR TreeFam; TF300479; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000020112; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR016528; VPS11.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR PIRSF; PIRSF007860; VPS11; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|PIRNR:PIRNR007860};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR007860};
KW Endosome {ECO:0000256|PIRNR:PIRNR007860};
KW Lysosome {ECO:0000256|PIRNR:PIRNR007860};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR007860};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR007860};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Transport {ECO:0000256|PIRNR:PIRNR007860};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 807..846
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 925 AA; 105771 MW; 4F6C115AE7132E00 CRC64;
MAAFLQWRKF VFFDKDTVKD PVDNGKNFVL PNGISACDSG RGHIVLGDMD GKIYLLTRSL
QLTSFQAYKL RVTHLYQLRQ HSILVSVGQD EQGINPLVKV WNLEKRDSGN PLCTRIFPAI
PGNKPTEVSC LGVHENLNFM AIGFTDGSVV LTKGDITRDR HSKTLTLHEG TSPVTGLAFR
QVAKVTHLFV ATLETVHCYT LSIKEYPKVE LDTHGCALGC SSLADPSQDS QFIVAGEECV
YLYQPDERGP CFAFDGHKLL AHWHRGYLFL LNRDAKSSNK TEFGSSSPSD KQLLTIYDLD
NKFIAYSASF DDVIDVVAEW GSFYILTRDG RMSVLQEKDT QTKLEMLFKK NLFVMAINLA
KGQHLDSDGL SEIFRQYGDH LYLKGDHDGA IQQYIRTIGK LEPSYVIRKF LDAQRIHNLT
AYLQALHRQS LANADHTTLL LNCYTKLKDS SKLEEFIKSN ESEVHFDVEI AIKVLRQAGY
HSHAVFLAEK HMHHEWYMKI QLEDLKNYQE GLRYIGRLPF EQAESNMKRY GKTLMHHVPE
GTTLLLKGLC TNYQPSTDAT ERDSLDRGRA NKANSEEFIP IFANNPRELK AFLEHMMDVD
SRCPQGVYDT LLELRLQDWA HEQDPVRKKV LQGEAVSLLR SDSTVFDKAL VLCQMHNFKE
GVLYLYEKGK LYQQIMHYHM QNEEYGKVVE ACQLYGDQEG CLWEQALGYF ARKEEDCKAY
ISEVLHHIDQ NNLMPPLLAT VVQTLAHNSS ATLSVIKDYL INKLQRESQQ IEDDERKICQ
YREETAHLRS EIEELKTSAK IFQKTKCNMC NSPLELPSVH FLCSHSFHQH CFENYAESEA
ECPTCTPGNR KVMDMLRAQD QKRDLHDHFN RQLRSSNDGF SVVADYFGRG VFNKLTLITD
PPGSKTGSLE VNLQRDLLIH TKRNC
//