ID   VAC14_XENLA             Reviewed;         782 AA.
AC   Q68F38;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Protein VAC14 homolog;
GN   Name=vac14;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-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; BC080007; AAH80007.1; -; mRNA.
DR   RefSeq; NP_001087491.1; NM_001094022.1.
DR   AlphaFoldDB; Q68F38; -.
DR   IntAct; Q68F38; 1.
DR   MaxQB; Q68F38; -.
DR   DNASU; 447315; -.
DR   GeneID; 447315; -.
DR   KEGG; xla:447315; -.
DR   CTD; 447315; -.
DR   Xenbase; XB-GENE-975924; vac14.L.
DR   OrthoDB; 306227at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 447315; Expressed in brain and 19 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070772; C:PAS complex; IEA:InterPro.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:InterPro.
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..782
FT                   /note="Protein VAC14 homolog"
FT                   /id="PRO_0000300490"
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          440..477
FT                   /note="HEAT 5"
FT   REPEAT          560..598
FT                   /note="HEAT 6"
FT   REGION          334..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  88917 MW;  9CEE8283D90DF1A2 CRC64;
     MNAERDLSPL TPNIVRALND KMYEKRKVAA LEIEKLVREF VSQNNTAQIK HVIQILSQEF
     ALSQHPHSRK GGLIGLAACS IALGKDSGQY LRELIEPVLT CFNDADSRLR YYACEALYNI
     VKVARGSVLP HFNVLFDGLS KLAADPDPNV KSGSELLDRL LKDIVTESSK FDLVGFVPLL
     RERIYSNNQY ARQFIISWIL VLESVPDINL LDYLPEILDG LFQILGDNSK EIRKMCEVSL
     GEFLKEIKKL PDSVKFAEMA NILVIHCQST DDLIQLTAMT WMREFLQLAG RVMLPYSSGI
     LTAVLPCLSY DDRKKNIKEV ANVCNQSLMK LITPEDDETD EVRQSPATQP DEDFSSNHEN
     SSQHTTYNRT LPSAPDSSLD NANIFAPSSM NTCPVSLNLD GIVHVLDRHL HESTTGMMTR
     ICVLKWLYHL YIKTPRKMFR HTDSLFPILL KTLSDESDEV ILKDLEVLAE IASSPAGQTD
     IVTDCNDLPT GMSELHVPVP TKVTQAHGSV IRGLECSPST PTMNSYFHRF MVNLLKRFSN
     ERKLLEIRGA FIIRQLCLLL NAENIFHSMA DILLREEDLK FASTMVQNLN SILLTSSELF
     QLRSQLKDLQ TPESCNLFCC LYRSWCHNPV ATVSLCFLTQ NYQHAYNLIQ KFGDLEVTVD
     FLTEVDKLVQ LIECPIFTYL RLQLLDVENN PYLIRALYGL LMLLPQSSAF QLLSHRLQCV
     PNPQLMRPGH KQEESSRAPK EDPARIDYVE LLQHFEKVQN KHLEIRHQRS GAGELLERRL
     VQ