VAC14_BOVIN
ID VAC14_BOVIN Reviewed; 783 AA.
AC A2VE70;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Protein VAC14 homolog;
GN Name=VAC14;
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].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scaffold protein component of the PI(3,5)P2 regulatory
CC complex which regulates both the synthesis and turnover of
CC phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes
CC into a star-shaped structure and nucleates the assembly of the complex.
CC The pentamer binds a single copy each of PIKFYVE and FIG4 and
CC coordinates both PIKfyve kinase activity and FIG4 phosphatase activity,
CC being required to maintain normal levels of phosphatidylinositol 3-
CC phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate
CC (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier
CC vesicles (ECV) / multivesicular bodies (MVB) transport intermediates
CC from early endosomes. {ECO:0000250|UniProtKB:Q08AM6}.
CC -!- SUBUNIT: Forms pentamers. Component of the PI(3,5)P2 regulatory
CC complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14.
CC VAC14 nucleates the assembly of the complex and serves as a scaffold by
CC pentamerizing into a star-shaped structure, which can bind a single
CC copy each of PIKFYVE and FIG4 and coordinates their activities.
CC Interacts with NOS1. {ECO:0000250|UniProtKB:Q08AM6}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q08AM6}.
CC Microsome membrane {ECO:0000250|UniProtKB:Q80W92}. Note=Mainly
CC associated with membranes of the late endocytic pathway.
CC {ECO:0000250|UniProtKB:Q08AM6}.
CC -!- DOMAIN: The C-terminal domain (residues 523-782) mediates pentameric
CC interactions and is necessary for the formation and maintenance of the
CC PI(3,5)P2 regulatory complex. {ECO:0000250|UniProtKB:Q08AM6}.
CC -!- SIMILARITY: Belongs to the VAC14 family. {ECO:0000305}.
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DR EMBL; BC133600; AAI33601.1; -; mRNA.
DR RefSeq; NP_001075913.1; NM_001082444.1.
DR AlphaFoldDB; A2VE70; -.
DR BioGRID; 189801; 1.
DR STRING; 9913.ENSBTAP00000032574; -.
DR PaxDb; A2VE70; -.
DR PRIDE; A2VE70; -.
DR GeneID; 533202; -.
DR KEGG; bta:533202; -.
DR CTD; 55697; -.
DR eggNOG; KOG0212; Eukaryota.
DR InParanoid; A2VE70; -.
DR OrthoDB; 306227at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000306; C:extrinsic component of vacuolar membrane; IBA:GO_Central.
DR GO; GO:0070772; C:PAS complex; IBA:GO_Central.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026825; Vac14.
DR InterPro; IPR021841; VAC14_Fig4p-bd.
DR PANTHER; PTHR16023; PTHR16023; 1.
DR Pfam; PF11916; Vac14_Fig4_bd; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Endosome; Membrane; Microsome;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..783
FT /note="Protein VAC14 homolog"
FT /id="PRO_0000300484"
FT REPEAT 5..42
FT /note="HEAT 1"
FT REPEAT 89..126
FT /note="HEAT 2"
FT REPEAT 171..208
FT /note="HEAT 3"
FT REPEAT 212..249
FT /note="HEAT 4"
FT REPEAT 439..476
FT /note="HEAT 5"
FT REPEAT 561..599
FT /note="HEAT 6"
FT REGION 331..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..778
FT /note="Mediates interaction with the PDZ domain of NOS1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q08AM6"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AM6"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AM6"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AM6"
SQ SEQUENCE 783 AA; 87843 MW; 1F345ECC7A9FC437 CRC64;
MNPEKDFAPL TPNIVRALND KLYEKRKVAA LEIEKLVREF VAQNNTVQIK HVIQTLSQEF
ALSQHPHSRK GGLIGLAACS IALGKDSGLY LKELIEPVLT CFNDADSRLR YYACEALYNI
VKVARGAVLP HFNVLFDGLS KLAADPDPNV KSGSELLDRL LKDIVTESNK FDLVGFIPLL
RERIYSNNQY ARQFIISWIL VLESVPDINL LDYLPEILDG LFQILGDNGK EIRKMCEVVL
GEFLKETKKS PSSVKFAEMA NILVIHCQTT DDLIQLTAMC WLREFIQLAG RVMLPYSSGI
LTAVLPCLAY DDRKRNIKEV ASVCNQSLMK LVTPEDDEPD EPRPVVQKQA GPSPEDCAAK
QEGAASGGPD GSCDSSFSSG ISVFTPASAE RAPVTLHLDG IVQVLNCHLS DTAIGMMTRI
AVLKWLYHLY IKTPRKMSRH TDSLFPVLLQ TLSDESDEVI LKDLEVLAEI ASSPAGQTDD
PGPLDGPDLR VSHSELQAPI PGRAGLLNTP GTKGLECSPS TPTMNSYFYK FMINLLKRFS
SERKLLEVRG AFIIRQLCLL LHAESIFHSM ADILLREEDL TFASTMVHTL NTILLTSTEL
FQLRNQLKDL KTPESRNLFC CLYRSWCHKP VTTVSLCFLT QNYRHAYDLI QKFGDLEVTV
DFLTEVDKLV QLIECPIFTY LRLQLLDVKS NPYLIKALYG LLMLLPQSSA FQLLSHRLQC
VPNPELLQTE DGLKAAPKSQ KADSPSIDYA ELLQHFERVQ KKHLEVRHQR SGRGDHLDRR
VVL
