ID   VAC14_CHICK             Reviewed;         780 AA.
AC   Q5ZIW5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein VAC14 homolog;
GN   Name=VAC14; ORFNames=RCJMB04_23c3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720669; CAG32328.1; -; mRNA.
DR   RefSeq; NP_001025735.1; NM_001030564.1.
DR   AlphaFoldDB; Q5ZIW5; -.
DR   STRING; 9031.ENSGALP00000003869; -.
DR   PaxDb; Q5ZIW5; -.
DR   GeneID; 415678; -.
DR   KEGG; gga:415678; -.
DR   CTD; 55697; -.
DR   VEuPathDB; HostDB:geneid_415678; -.
DR   eggNOG; KOG0212; Eukaryota.
DR   InParanoid; Q5ZIW5; -.
DR   OrthoDB; 306227at2759; -.
DR   PhylomeDB; Q5ZIW5; -.
DR   PRO; PR:Q5ZIW5; -.
DR   Proteomes; UP000000539; 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   Endoplasmic reticulum; Endosome; Membrane; Microsome; Reference proteome;
KW   Repeat.
FT   CHAIN           1..780
FT                   /note="Protein VAC14 homolog"
FT                   /id="PRO_0000300488"
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          438..475
FT                   /note="HEAT 5"
FT   REPEAT          558..596
FT                   /note="HEAT 6"
FT   REGION          348..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  87823 MW;  DDF6626F1002BDF4 CRC64;
     MNAERDLAPL APSVVRALND KLYEKRKVAA LEIEKLVREF VAQNNTSQVK HVILILSQEF
     ALSQHPHSRK GGLIGLAACS IALGKDSGLY LKELIEPVLT CFNDADSRLR YYACEALYNI
     VKVARGSVLP HFNVLFDGLS KLAADPDPNV KSGSELLDRL LKDIVTESNQ FDLVGFIPLL
     RERIYSNNQY ARQFIISWIL VLESVPDINL LDYLPEILDG LFQILGDNSK EIRKMCEVAL
     GEFLKEIKKN PSSVKFAEMA NILVIHCQAA DDLIQLTAMC WMREFIQLAG RVMLPYSSGI
     LTAVLPCLSY DDRKKNIKEV ANVCNQSLMK LVIPEDDEMD EAKQSITLSA EPNPEEPVSK
     PEAASTGSLD VSGDSSVSNA SVCTVTSSER IQVTLNLDGI VQVLDCHLHD TSIGMMTRIA
     VLKWLYHLYI KTPRKMFRHT DSLFPILLRT LSDESDEVIL KDLEVLAEIA SSPAGQTEGY
     GPSEAAEPRP GQVELHVPIR NSQLSSSGPK GLECSPSTPT MNSYFYKFMI NLLKRFSSER
     KLLETRGAFI IRQLCLLLNT ENIFHSMADI LLREEDLKFA STMVHTLNTI LLTSSELFQL
     RNQLKDLRTP ESRNLFCCLY RSWCHNPVTT VSLCFLTQNY KHAYDLIQKF GDLEVTVDFL
     TEVDKLVQLI ECPIFTYLRL QLLDVKNNPY LIKALYGLLM LLPQSSAFQL LSHRLQCVPN
     PELMQSADGS RASASSRRPA SSTIDYTELL QHFDKVQSKH LEVRHQRAGR AEQPERRVVL