ID   SRAC1_BOVIN             Reviewed;         654 AA.
AC   Q2TBM9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Protein SERAC1;
DE   AltName: Full=Serine active site-containing protein 1;
GN   Name=SERAC1;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BC109896; AAI09897.1; -; mRNA.
DR   RefSeq; NP_001033639.1; NM_001038550.2.
DR   RefSeq; XP_005211129.1; XM_005211072.3.
DR   RefSeq; XP_010807020.1; XM_010808718.2.
DR   AlphaFoldDB; Q2TBM9; -.
DR   STRING; 9913.ENSBTAP00000015295; -.
DR   ESTHER; bovin-srac1; PGAP1.
DR   PaxDb; Q2TBM9; -.
DR   PRIDE; Q2TBM9; -.
DR   Ensembl; ENSBTAT00000015295; ENSBTAP00000015295; ENSBTAG00000011509.
DR   Ensembl; ENSBTAT00000075870; ENSBTAP00000057129; ENSBTAG00000011509.
DR   GeneID; 519860; -.
DR   KEGG; bta:519860; -.
DR   CTD; 84947; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011509; -.
DR   VGNC; VGNC:34460; SERAC1.
DR   eggNOG; KOG2029; Eukaryota.
DR   GeneTree; ENSGT00390000003560; -.
DR   HOGENOM; CLU_023317_1_0_1; -.
DR   InParanoid; Q2TBM9; -.
DR   OMA; RRTEYIY; -.
DR   OrthoDB; 1311762at2759; -.
DR   TreeFam; TF319689; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000011509; Expressed in spermatid and 104 other tissues.
DR   ExpressionAtlas; Q2TBM9; baseline.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0032367; P:intracellular cholesterol transport; IEA:Ensembl.
DR   GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Mitochondrion; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..654
FT                   /note="Protein SERAC1"
FT                   /id="PRO_0000274670"
FT   TRANSMEM        32..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   654 AA;  74196 MW;  E75298FC8A593D98 CRC64;
     MSLAAYCVIC CRRMGTSTPP PKSSTYWRDI RNIIKFTGSL ILGGSLFITY EVLALKKSLT
     LDTQVIEREK MKSYIYVHTV SLDKTENHGI TYQARKELHK AVRKVLATSA RIFRGPFADT
     FSTVDIEDHD CAVWLLLRKS RSDDRAARLQ AVQEMSEARH WHDYQYRIIA QACDMRTLTG
     LARSKDSDLR FFLRPPPLPS LKEDSSTEEE LRHLLASLPQ TDLDECIQCF TALALSESSQ
     SLAAQKGGLW CFGGNGLPYA ESFGEVPSAT VEMFCLEALV KHSEIPTHCD KIEANGGLQL
     LQRLYQLHKD CPKVQRNIMR ILGNMALNEH LHSTIVRSGW VSILAEAIKS QHIMEASHAA
     RTLANLDRET VPDKYHDGVY VLHPQYRTSQ PIKADVLFIH GLMGAAFKTW RQQDNDQDLT
     EKVSEDETKY TTCWPKSWLA RDCPALRIIS VEYDTSLSDW RARCPTERKS IAFRSNELLR
     KLRAAGVGDR PVVWVSHSMG GLLVKKMLLE ASKRPEMNTI INNTRGIIFY SVPHHGSHLA
     EYSVNIRYLL FPSLEVKELS KDSPALKTLQ DDFLEFAKDK NFQVLSFVET LPTYIGSMIK
     LHVVPLDSAD LGLGDLIPVD VNHLNICKPK KKDAFLYQRT LQFIRDALAK DLEN