ID H2MIL7_ORYLA Unreviewed; 682 AA.
AC H2MIL7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Protein SERAC1 {ECO:0000256|ARBA:ARBA00040991};
DE AltName: Full=Serine active site-containing protein 1 {ECO:0000256|ARBA:ARBA00041701};
GN Name=serac1 {ECO:0000313|Ensembl:ENSORLP00000018499.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000018499.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000018499.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018499.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000018499.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000018499.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037251}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the SERAC1 family.
CC {ECO:0000256|ARBA:ARBA00038024}.
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DR RefSeq; XP_011489946.1; XM_011491644.1.
DR AlphaFoldDB; H2MIL7; -.
DR STRING; 8090.ENSORLP00000018499; -.
DR Ensembl; ENSORLT00000018500.2; ENSORLP00000018499.2; ENSORLG00000014762.2.
DR eggNOG; KOG2029; Eukaryota.
DR GeneTree; ENSGT00390000003560; -.
DR InParanoid; H2MIL7; -.
DR TreeFam; TF319689; -.
DR Proteomes; UP000001038; Chromosome 24.
DR Bgee; ENSORLG00000014762; Expressed in animal zygote and 14 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 682 AA; 76604 MW; A6ED103FA0298990 CRC64;
MSVAALRLIR CRKLSTAGPP GVNKVLQWKD LRKVAKVTGA VILGGCLFIT YEMVALEKAV
TIDTSAVLQE KYKSYIYLKA TPAAEKENLT AGLIYKARKE LHKAARRFME ASSRLFLQSL
DEHLSHVDAD PHEVALWVLL KQTQSANKAI RLQAVQELAD NHHWHAYQYQ TAAQVIDQRT
AVGLARTPHV DLRFFRQPPA LPDLEDVCTT NEDIFWECLP NSNAKPSSQG TSVEEGLWQL
LASLPQSEVD KCVQYFTSLA LRESTQSMAA QRGGLWCFGG NGLPYAQSLT SVPSEKVESF
CLQALVQHSK VQSHCDHIVA KGGLLLLQRI YQLRRDSPKI QRNIIRIIGN LALNESVHRD
IVQSGWLSIL AEMMQSPHVT QVSFAARALA NLDRESVVEK YQDGVYILHP QTRNGQPVKA
DVLFIHGILG AAFKTWRQKD SSLQQEETEM ESRSDYTECW PKSWLAEDCP NLRVLSVEYD
SHLSDWMSKC PAENQRKSLA YRSQELLKKL KQAGVGERPV VWVAHSMGGL LVKKMLLDAS
EDPEMKGLLK NTRGVLFYSV PHHGTFMAEY SVNVRYLLFP SIEVRELCKD SPALSSLNES
FVNIAKENDF KVMSFAESQA TNVGPMIKIV VVPKQSADLG IGELVEVNVD HLNICKPEKK
DSFLYKRSLQ FIQEALQSFS SQ
//
