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Database: UniProt
Entry: A0A087VB28_BALRE
LinkDB: A0A087VB28_BALRE
Original site: A0A087VB28_BALRE 
ID   A0A087VB28_BALRE        Unreviewed;       881 AA.
AC   A0A087VB28;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Vacuolar protein sorting-associated protein 11 homolog {ECO:0000256|PIRNR:PIRNR007860};
GN   ORFNames=N312_05425 {ECO:0000313|EMBL:KFO09820.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO09820.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO09820.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO09820.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL486627; KFO09820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087VB28; -.
DR   Proteomes; UP000053309; Unassembled WGS sequence.
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   SMART; SM00184; RING; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053309};
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          762..800
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          712..753
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   881 AA;  101480 MW;  C309641E1FCEB087 CRC64;
     MEGQIWFLPR SLQLSSFQAY KLRVTHLYQL KQHSILVSVG EDEEGINPLV KVWNLEKRDG
     GNPLCTRIFP AIPGNKPTVV SCLTVHENLN FMAIGFADGS VVLTKGDITR DRHSKTQILR
     EGSYPVTGLA FRQSGKTTHL FVVTTENIQS YMLSVKDYPH LELDTHGCGL RCSSLSDPSQ
     DLQFIVAGNE CVYLYQPDER GPCFAFEGQK LIVHWYRGYL IIVSKDRKTS PKSEFAGNEA
     QNSDKQVLNI YDLCNKFIAY SSIFDDIVDV LAEWGSLYVL TRDGKIHVLQ EKDTQTKLEA
     RKSMLFRKNL FEMAINLAKS HHLDSDGLSE IFRQYGDHLY NKGNHDGAIQ QYIRTIGKLE
     PSYVIRKFLD AQRIHNLTAY LQTLHLQSLA NADHTTLLLN CYTKLKDSSK LEEFIKTSES
     EVRFDVETAI KVLRQAGYYS HAVYLAEKHA HHEWYLKIQL EDIKNYQEAL RYIGKLPFDQ
     AESNMKRYGK ILMHHVPNET TELLKILCTD YRPLGDSEGP GMLEGKKANS EEFIPVFANN
     SRELKAFLEH MTEVQADSPQ GVYDTLLELR LQNWAHEQDE QVKEKLHNEA LTLLKSGRFK
     TVFDKALVLC QMHNFKDGVL YLYEQGKLFQ QIMHYHMQNE QYKKVIEVCE LYGDQEACLW
     EQALGYFARK EEDCKEYIAA VLKHIENKNL MPPLLVVQTL AHNSTATLSV IKDYLVNKLQ
     KQSRQIEQDE QRIQKYREET TRIRQEIEEL KASPKIFQKT KCSICTSALE LPSVHFLCGH
     SFHQHCFESY SESDSECPTC MPENRKVMDM IRAQEQKRDL HDQFQHQLKC SNDGFSVVAD
     YFGRGVFNKL TLITDLPSGK TATTIEAGLQ RELLMHTKRS T
//
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