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Database: UniProt
Entry: B9T8N6_RICCO
LinkDB: B9T8N6_RICCO
Original site: B9T8N6_RICCO 
ID   B9T8N6_RICCO            Unreviewed;       962 AA.
AC   B9T8N6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Vacuolar protein sorting-associated protein 11 homolog {ECO:0000256|PIRNR:PIRNR007860};
GN   ORFNames=RCOM_0416040 {ECO:0000313|EMBL:EEF27778.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- FUNCTION: Involved in regulating membrane fusion at the tonoplast and
CC       the prevacuolar compartment. {ECO:0000256|PIRNR:PIRNR007860}.
CC   -!- SUBUNIT: Core component of at least two putative endosomal tethering
CC       complexes, the homotypic fusion and vacuole protein sorting (HOPS)
CC       complex and the class C core vacuole/endosome tethering (CORVET)
CC       complex. {ECO:0000256|PIRNR:PIRNR007860}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|PIRNR:PIRNR007860};
CC       Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007860}.
CC       Prevacuolar compartment membrane {ECO:0000256|PIRNR:PIRNR007860};
CC       Peripheral membrane protein {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; EQ975130; EEF27778.1; -; Genomic_DNA.
DR   RefSeq; XP_002534605.1; XM_002534559.2.
DR   AlphaFoldDB; B9T8N6; -.
DR   STRING; 3988.B9T8N6; -.
DR   GeneID; 8287949; -.
DR   KEGG; rcu:8287949; -.
DR   eggNOG; KOG2114; Eukaryota.
DR   InParanoid; B9T8N6; -.
DR   OrthoDB; 5491867at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR   GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   CDD; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
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   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; PF17122; zf-C3H2C3; 1.
DR   PIRSF; PIRSF007860; VPS11; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR007860};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Vacuole {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          858..893
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          815..849
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   962 AA;  108459 MW;  8E421A35DD81C90C CRC64;
     MYQWRKFEFF EEKYGGKSKI PEDVSGNINC CSSGRGKVVI GSDEGHVSLL DRGLHFNFSF
     LAHSSSVLFL QQLKQRNFLV TVGEDEQIAP QQSAMCLKVF DLDKMQPEGT SSIVPDCIGI
     LRIFTNQFPH AKITSFLVLE EAPPILLIAI GLDNGCIYCI KGDIARERIT RFKLQIDNNN
     VSDKSSSSIT GLGFRVDGQA LQLFAVSPNS VSLFSLQSQP PRRQLLDQIG CNVNSVAMSD
     RSELIIGRPE AVYFYEVDGR GPCWAFEGEK KFVGWFRGYL LCVIGDQRSG KDTFNIYDLK
     NRLIAHSLAV KEVSHMLCEW GNIILIMNDK SALCIGEKDM ESKLDMLFKK NLYTVAINLV
     QSQQADAAAT AEVLRKYGDH LYSKQDYDEA MAQYISTIGH LEPSYVIQKF LDAQRIYNLT
     NYLENLHEKG LASKDHTTLL LNCYTKLKDV DKLNVFIKSE DGVGEHKFDV ETAIRVCRAA
     NYHEHAMYVA KKAGRHELYL KILLEDLGRY DEALQYISSL EPSQAGVTVK EYGKILIEHK
     PAETIEILMR LCTEDGESAK RGSSSGAYLS MLPSPVDFLN IFIHHPQSLM NFLEKYTDKV
     KDSPAQVEIH NTLLELYLSN EMNFPAVSQA SNGVDISLQA KSGAGRKSKA KSNGKVIADR
     KDIYKEKDRV ERQEKGLLLL KSAWPADQEH PLYDVDLAII LSEMNAFKEG LLYLYEKMKL
     YKEVIACYMQ AHDHEGLIAC CKRLGDSSKG GEPSLWADLL KYFGELGEDC SKEVKEVLTY
     IERDDILPPI IVLQTLSRNP CLTLSVIKDY IARKLEQESK LIEEDRQAID KYQEDTLAMR
     KEIHELRTNA RIFQLSKCTA CTFTLDLPAV HFMCMHSFHQ RCLGDNEKEC PECAPEYRAV
     MEMKRSLEQN SKDQDQFFQL VKGSKDGFSV IAEYFGKGII SKTSNGTSGA LRSGSTSSSS
     GF
//
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