VAC14_DANRE
ID VAC14_DANRE Reviewed; 771 AA.
AC Q66L58;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein VAC14 homolog;
GN Name=vac14; ORFNames=zgc:100945;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) 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; BC078425; AAH78425.1; -; mRNA.
DR RefSeq; NP_001004650.1; NM_001004650.1.
DR AlphaFoldDB; Q66L58; -.
DR STRING; 7955.ENSDARP00000003288; -.
DR PaxDb; Q66L58; -.
DR Ensembl; ENSDART00000009767; ENSDARP00000003288; ENSDARG00000014303.
DR GeneID; 447912; -.
DR KEGG; dre:447912; -.
DR CTD; 55697; -.
DR ZFIN; ZDB-GENE-040912-82; vac14.
DR eggNOG; KOG0212; Eukaryota.
DR GeneTree; ENSGT00390000008385; -.
DR InParanoid; Q66L58; -.
DR OMA; TYLRMQL; -.
DR PhylomeDB; Q66L58; -.
DR TreeFam; TF343690; -.
DR PRO; PR:Q66L58; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000014303; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; Q66L58; baseline.
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 Endoplasmic reticulum; Endosome; Membrane; Microsome; Reference proteome;
KW Repeat.
FT CHAIN 1..771
FT /note="Protein VAC14 homolog"
FT /id="PRO_0000300489"
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 442..479
FT /note="HEAT 5"
FT REPEAT 550..588
FT /note="HEAT 6"
FT REGION 334..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 87557 MW; 72E9733274E2727D CRC64;
MNTEKDFSPL TPNIVRALND KLYEKRKVAA LEIEKLVREF VAQNNSAQIR HVIQILATEF
ALSQHPHSRK GGLIGLAACS IALGKDSGLY LKELIDPVLT CFNDSDSRLR YYACEALYNI
VKVARGAVLP HFNVLFDGLS KLAADPDPNV KSGSELLDRL LKDIVTESNK FDLVAFVPLL
RERIYSNNQY ARQFIISWIH VLESVPDINL LDYLPEILDG LFQILGDSSK EIRRMCELVL
GEFLKEIKKN PSSVKFAEMA NILVIHCQVS DESKSTNDLI QLTSMTWMRE FIQLAGRVVL
PYSSGILTAV LPCLSYDDRK KSTKEAASAC NHSLMKLVTP EDDEDDEESQ TKSSPPSDEA
PSKKEGDLND SLNESQESVG FSNISFFTPA SSDRSAVTLD LDGIVQVLDR HLHDSSTGMM
TRIAVLKWLY HLYIKTPRKM FKHTDSLFPM LLKTLSDESD EVILKDLEVL AEIASSPAGQ
TDTSGSCDIS DSKTELHIPG SKMTDLSPST PSMNSYFYKF MINLLKRFSL ERKLLEMRGA
FIIRQLCLLL HAENIFHSMA DILLKEEDLK FASTMVQTLN TILLTSAELF QLRNQLKDLR
TQESCALFCC LYRSWCHNPV ATVSLCFLTQ NYRHAYDLIQ KFGDLEVTVD FLMEVDKLVQ
LIESPIFTYL RLQLLDVEHN PYLIKALYGL LMLLPQSQAF QLLSHRLSCV PNPELMRTLE
DQKVAVKDKH LAQPHIDYSE LLQHFDRVQS KHLEVRHQRT GRSEHPDRKL M
