ID A0A452GTD1_9SAUR Unreviewed; 815 AA.
AC A0A452GTD1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Vacuolar protein sorting-associated protein 16 homolog {ECO:0000256|ARBA:ARBA00017947, ECO:0000256|PIRNR:PIRNR007949};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000005293.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000005293.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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:PIRNR007949}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000256|ARBA:ARBA00004412}.
CC Late endosome membrane {ECO:0000256|PIRNR:PIRNR007949}; Peripheral
CC membrane protein {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 STRING; 38772.ENSGAGP00000005275; -.
DR Ensembl; ENSGAGT00000006140.1; ENSGAGP00000005275.1; ENSGAGG00000004273.1.
DR Ensembl; ENSGAGT00000006151.1; ENSGAGP00000005286.1; ENSGAGG00000004273.1.
DR Ensembl; ENSGAGT00000006160.1; ENSGAGP00000005293.1; ENSGAGG00000004273.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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: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 InterPro; IPR036322; WD40_repeat_dom_sf.
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.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Transport {ECO:0000256|PIRNR:PIRNR007949}.
FT DOMAIN 1..395
FT /note="Vps16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04841"
FT DOMAIN 493..811
FT /note="Vps16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04840"
FT COILED 325..352
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 815 AA; 93256 MW; E1E87B7C09052016 CRC64;
MAWNLKEDLR DCLVAAAPYG GPIALLKNNF RKEKSLGSRP LLEIYSASGV PLASVLWKSG
QVVQLGWTAS EDLLCIQEDG TVLIYNLFCE FKRHFSMGNE VLQNHVREAK VFHTEYGTGV
AILTGAHRFS LTTNIDDLKL RRMPEVPGLQ KLPSCWAVLS QDRVTIILLA VGQDLYLLDN
TSCSVVTPPG ISAHAGAYVQ MAVSFNYRYL ALFTDTGSIW MGTSSLKEKL GEFSCDFRAP
PRQMVWCTRP RSKQRAVVVA WDRRLLVAGN SKECIQFVLD EDSYLVPELD GVRIFSCTTH
EFLHEIPEAS EEIFKIASMA PGALLLEAQR EYEKQSQKAD EYLREIKDQN LLAEAVRQCI
EAAGYEHEPE TQKSLLRAAS FGKCFLDKFP SESFVWTCRD LRVLNAIRDY QIGIPLTFAQ
YKQLTIEVLL DRLVLRRLYP LAIKICEYLR LSEFQGVSRI LAHWACYKVQ QKDKSDEEVA
HAINQKLGDT PGISYSEIAA RAYDCGRTEL AIKLLEYEPR SGEQVPLLLK MKKSQLALNK
AIESGDTDLV YTVVLHLKNE LNRGTFFMTL QKQPVALSLY RQFCKHQELE TLKDLYNQDD
DHQELGNFHV HSSYSSEKRI EGRVGALQNA VDEYYKAKNE FAAKATEDQI KLLRMQRRLQ
DELDKPYVDY SLHDTVYSLI LDGNHKRAEQ LYRDFRIPDK RFWWLKISAL AEREDWEEME
KFSKSKKSPI GYLPFVEICM KHHNRHEAKK YAARVTPEQR VKAHILVREL DQAADAAIEH
KNENEMNLVL SKCTAATDSL VVEKINRAKA QTLKK
//
