ID A0A182K7D2_9DIPT Unreviewed; 835 AA.
AC A0A182K7D2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE RecName: Full=Vacuolar protein sorting-associated protein 16 homolog {ECO:0000256|ARBA:ARBA00017947, ECO:0000256|PIRNR:PIRNR007949};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR006667-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR006667-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR006667-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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:PIRNR007949}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000256|PIRNR:PIRNR007949}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR007949}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR007949}. Lysosome membrane
CC {ECO:0000256|PIRNR:PIRNR007949}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR007949}; Cytoplasmic side
CC {ECO:0000256|PIRNR:PIRNR007949}. Note=Cytoplasmic, peripheral membrane
CC protein associated with late endosomes/lysosomes.
CC {ECO:0000256|PIRNR:PIRNR007949}.
CC -!- SIMILARITY: Belongs to the VPS16 family.
CC {ECO:0000256|ARBA:ARBA00009250, ECO:0000256|PIRNR:PIRNR007949}.
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DR AlphaFoldDB; A0A182K7D2; -.
DR STRING; 43041.A0A182K7D2; -.
DR EnsemblMetazoa; ACHR006667-RA; ACHR006667-PA; ACHR006667.
DR VEuPathDB; VectorBase:ACHR006667; -.
DR OrthoDB; 1110811at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
DR GO; GO:0033263; C:CORVET complex; IEA:UniProtKB-UniRule.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007033; P:vacuole organization; IEA:InterPro.
DR Gene3D; 1.10.150.780; Vps16, C-terminal region; 1.
DR InterPro; IPR016534; VPS16.
DR InterPro; IPR006925; Vps16_C.
DR InterPro; IPR038132; Vps16_C_sf.
DR InterPro; IPR006926; Vps16_N.
DR PANTHER; PTHR12811; VACUOLAR PROTEIN SORTING VPS16; 1.
DR PANTHER; PTHR12811:SF0; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 16 HOMOLOG; 1.
DR Pfam; PF04840; Vps16_C; 1.
DR Pfam; PF04841; Vps16_N; 1.
DR PIRSF; PIRSF007949; VPS16; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|PIRNR:PIRNR007949};
KW Lysosome {ECO:0000256|PIRNR:PIRNR007949};
KW Membrane {ECO:0000256|PIRNR:PIRNR007949};
KW Protein transport {ECO:0000256|PIRNR:PIRNR007949};
KW Transport {ECO:0000256|PIRNR:PIRNR007949}.
FT DOMAIN 6..423
FT /note="Vps16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04841"
FT DOMAIN 519..828
FT /note="Vps16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04840"
SQ SEQUENCE 835 AA; 94405 MW; 7F65229910E6DCCF CRC64;
MSLLCNTGDW FTLGQGNAFR KIELYNMEWP GSINLENMVV YAAPYGGPIA VVKDPKLFIK
LDGGTSTRPI IRIFNCVGKL ISSINWDCGN LVTLGWSDAE ELIGVQDDGT IFLHDMFGNF
VHKFSVGKDV TDVADARIFP SASGTGVAVM TSGFKIYILN NIKDPKSRPL SELLNLSSSL
TCWEMVCKDR TTSCLLAAGT EITIVRHGDN AFTNNTLTMR NEFQSISLLS VSFDHEHVAL
LTNTGCLWMG SWDLKHKYCE FVTGRQEKAK QLVWCIDGGT GYEAQAVIVS YMNLILIVGA
SGESSVYTYD SPMTLIPEMD CVRVLTNYYH ELIQKVPLST SKIFGINISE PASFLFEAHR
KFQDRSHQSD EYLCLIQNKL PTAVADCVEA AGHEFDPSTQ KSLIRAAYFG KSFISSYSCS
DYITMCKTLK VLNVLRDRIV GIPITIQQFN HLQPVVILDR LVFRKYYGLS IHIAKYLKLQ
ETRILEHWAF QKIVHDKNDD EVARKIAAKF SSAGLREPMS YANVADKAQQ IGKTKLAITL
LELETKKKLQ VPLLLKLGAC EKALIAATQS GDIDLIYMAI LEMKNTTALA KFHMTIRRYP
LAQNLYKKYC QLNSLSTLKD IHSQEDDFLS QAELALREAL QLGNLDASIP DISGNYRKAG
KTIEADLADE TKKLIRHQKL LQDKYQKDFF GLALHAMVRK LLQLGDQRYA EKLKSEFRMP
DRRFWWLRIQ SYADNYQWEE LEKFGKAKKS VIGYEPFVEV CLTKQNVTEA KKYLPRCSEE
NKLKWYLRAG CYADAATIAF MQKDIDSLLK IHDHCNDSAL MAKVENMIGQ LSSKK
//