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VPS16_BOVIN
ID   VPS16_BOVIN             Reviewed;         839 AA.
AC   Q5E9L7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Vacuolar protein sorting-associated protein 16 homolog;
GN   Name=VPS16;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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 which are
CC       proposed to be involved in the Rab5-to-Rab7 endosome conversion
CC       probably implicating MON1A/B, and via binding SNAREs and SNARE
CC       complexes to mediate tethering and docking events during SNARE-mediated
CC       membrane fusion. The HOPS complex is proposed to be recruited to Rab7
CC       on the late endosomal membrane and to regulate late endocytic,
CC       phagocytic and autophagic traffic towards lysosomes. The CORVET complex
CC       is proposed to function as a Rab5 effector to mediate early endosome
CC       fusion probably in specific endosome subpopulations. Required for
CC       recruitment of VPS33A to the HOPS complex. Required for fusion of
CC       endosomes and autophagosomes with lysosomes; the function is dependent
CC       on its association with VPS33A but not VPS33B. The function in
CC       autophagosome-lysosome fusion implicates STX17 but not UVRAG.
CC       {ECO:0000250|UniProtKB:Q9H269}.
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. Their common core is composed of the class C Vps proteins
CC       VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with
CC       VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1. Interacts with
CC       RAB5C. Interacts with STX17, MON1B. Associates with adapter protein
CC       complex 3 (AP-3) and clathrin:AP-3 complexes (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H269}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9H269}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9H269}. Early endosome
CC       {ECO:0000250|UniProtKB:Q9H269}. Cytoplasmic vesicle, clathrin-coated
CC       vesicle. Cytoplasmic vesicle, autophagosome
CC       {ECO:0000250|UniProtKB:Q9H269}. Note=Colocalizes with AP-3, clathrin,
CC       Rab5 and Rab7b (By similarity). Cytoplasmic, peripheral membrane
CC       protein associated with early endosomes and late endosomes/lysosomes.
CC       {ECO:0000250|UniProtKB:Q9H269}.
CC   -!- SIMILARITY: Belongs to the VPS16 family. {ECO:0000305}.
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DR   EMBL; BT020903; AAX08920.1; -; mRNA.
DR   RefSeq; NP_001015522.1; NM_001015522.1.
DR   STRING; 9913.ENSBTAP00000001744; -.
DR   PaxDb; Q5E9L7; -.
DR   PRIDE; Q5E9L7; -.
DR   GeneID; 505361; -.
DR   KEGG; bta:505361; -.
DR   CTD; 64601; -.
DR   eggNOG; KOG2280; Eukaryota.
DR   InParanoid; Q5E9L7; -.
DR   OrthoDB; 1258856at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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; -; 1.
DR   InterPro; IPR016534; VPS16.
DR   InterPro; IPR006925; Vps16_C.
DR   InterPro; IPR038132; Vps16_C_sf.
DR   InterPro; IPR006926; Vps16_N.
DR   PANTHER; PTHR12811; PTHR12811; 1.
DR   Pfam; PF04840; Vps16_C; 1.
DR   Pfam; PF04841; Vps16_N; 1.
DR   PIRSF; PIRSF007949; VPS16; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Endosome; Lysosome; Membrane; Nitration;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..839
FT                   /note="Vacuolar protein sorting-associated protein 16
FT                   homolog"
FT                   /id="PRO_0000253018"
FT   REGION          642..736
FT                   /note="Interaction with VPS33A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H269"
FT   MOD_RES         4
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q920Q4"
SQ   SEQUENCE   839 AA;  94813 MW;  186D04C686CCE96B CRC64;
     MDCYTANWNP LGDSAFYRKY ELYSMDWDLK EELRDCLVAA APYGGPIALL RNPWRKEKPA
     SARPVLEIYS ASGVPLASLL WKSGPVVSLG WSAEEELLCV QEDGVVLVYG LHGDFRRHFS
     MGNEVLQNRV LDARIFHTEF GSGVAILTGA HRFTLSANVG DLKLRRMPEV PGLXSAPSCW
     TTVCQDRVAH ILLAVGPDLY LLDHAACSAV TPPGLAPGVS SFLQMAVSFT YRHLALFTDT
     GYIWMGTASL KEKLCEFNCN IRAPPKQMVW CSRPRSKERA VVVAWERRLM VVGDAPESIQ
     FVLDEDSYLV PELDGVRVFS RSTHEFLHEV PVASEEIFKI ASMAPGALLL EAQKEYEKES
     QKADEYLREI QELGQLPQAV QQCIEAAGHE HWPDMQKSLL RAASFGKCFL DRFPPDSFVR
     MCQDLRVLNA IRDYHIGIPL TYSQYKQLTI QVLLDRLVLR RLYPLAIQIC EYLRLPEVQG
     VSRILAHWAC YKVQQKDVSD EDVARAINQK LGDTPGVSYS DIAARAYGCG RTELAIKLLE
     YEPRSGEQVP LLLKMKRSKL ALSKAIESGD TDLVFTVLLH LKNELNRGDF FMTLRNQPMA
     LSLYRQFCKH QELETLKDLY NQDDNHQELG SFHIRASYAA EERIEGRVAA LQTAADAFYK
     AKNEFAAKAT EDQMRLLRLQ RRLEDELGGQ FLDLSLHDTV TTLILSGQNK RAEQLARDFR
     IPDKRLWWLK LTALADLEDW EELEKFSKSK KSPIGYLPFV EICMKQHNKY EAKKYASRVG
     PEQKVKALLL VGDVAQAADV AIEHRNEAEM SLVLSHCTGA TDGATADKIQ RARAQAQKK
 
 
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