ID   SRAC1_DANRE             Reviewed;         658 AA.
AC   Q5SNQ7; Q5SNQ8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Protein SERAC1;
DE   AltName: Full=Serine active site-containing protein 1;
GN   Name=serac1;
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 GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Plays an important role in the phosphatidylglycerol
CC       remodeling that is essential for both mitochondrial function and
CC       intracellular cholesterol trafficking. May catalyze the remodeling of
CC       phosphatidylglycerol and be involved in the transacylation-acylation
CC       reaction to produce phosphatidylglycerol-36:1. May be involved in
CC       bis(monoacylglycerol)phosphate biosynthetic pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250}.
CC       Mitochondrion {ECO:0000250}. Note=Localizes at the endoplasmic
CC       reticulum and at the endoplasmic reticulum-mitochondria interface.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SERAC1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI20612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL954831; CAI20612.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL954831; CAI20613.1; -; Genomic_DNA.
DR   RefSeq; XP_005160640.1; XM_005160583.3.
DR   AlphaFoldDB; Q5SNQ7; -.
DR   STRING; 7955.ENSDARP00000126448; -.
DR   ESTHER; danre-srac1; PGAP1.
DR   PaxDb; Q5SNQ7; -.
DR   Ensembl; ENSDART00000151950; ENSDARP00000126448; ENSDARG00000056121.
DR   Ensembl; ENSDART00000192269; ENSDARP00000147756; ENSDARG00000116580.
DR   GeneID; 568022; -.
DR   CTD; 84947; -.
DR   ZFIN; ZDB-GENE-040616-1; serac1.
DR   eggNOG; KOG2029; Eukaryota.
DR   GeneTree; ENSGT00390000003560; -.
DR   InParanoid; Q5SNQ7; -.
DR   OMA; RRTEYIY; -.
DR   OrthoDB; 1311762at2759; -.
DR   PhylomeDB; Q5SNQ7; -.
DR   TreeFam; TF319689; -.
DR   PRO; PR:Q5SNQ7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000056121; Expressed in mature ovarian follicle and 21 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Mitochondrion; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..658
FT                   /note="Protein SERAC1"
FT                   /id="PRO_0000274674"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   658 AA;  74438 MW;  2F935A4AAA373443 CRC64;
     MSVSALRLIR VRRLSTSGPA VKRALPWRDI RRIAKVTGAI VFGGCVFITY EVVTLNQALT
     IDTSAILQEK QKSYIYPTHS TNREQESLAS GLTIKTRREL HKAARKFLEI TSRVLHHPLD
     EHLSHLDADP HECALWVLLK RSRSADRAVR HLAVQELAHN HHWRDYQYQT AAQVVDQRTA
     VALARIPNVD LRFFLPPPPL PHTEDDISIE DGLRQLLASL PQSDVDQCVQ YFTSLALRES
     SQSLASQRGG LWCFGGNGLP YAQSLTSTPS EKVETFCLQA LVQHSKVRSH CEHIVANGGL
     QLLQRVYQLR RDSPKIQRNI VRIIGNLALN ENLHTTIVQS GWMSVLAEMI QSPHIMQASH
     AARALANLDR DAVRQKYQDG VYILHPQCRT NQPIKADVLF VHGLLGAAFK TWRQKDCDVT
     DDEKLEGVRE DYTECWPKSW LAADCPNLRI LSVEYDTHLS DWNSKCPVEN QRKSLAFRSQ
     ELLRKLKDAG VGERPVIWVA HSMGGLLVKK MLLDAAKDPD LSSLIKNTKG ILFYSVPHHG
     TFMAEYSVSV RYLLFPSIEV KELCRDSPAL RDLNENFLNI AKDREFKVLS FAETVPTYIG
     PMLKILVVPA HSADLGIGDL IQVDVDHLNI CKPEKKDTFL YKRTLQFIQD ALGGRRIK