SRAC1_MOUSE
ID SRAC1_MOUSE Reviewed; 654 AA.
AC Q3U213; Q3TS62; Q9D2G7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein SERAC1;
DE AltName: Full=Serine active site-containing protein 1;
GN Name=Serac1; Synonyms=D17Ertd141e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP VAL-4; PHE-6; PHE-7 AND THR-64.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, AND VARIANTS VAL-4; PHE-6; PHE-7; MET-25; THR-64 AND
RP SER-518.
RX PubMed=15722415; DOI=10.1073/pnas.0407970102;
RA Schimenti J.C., Reynolds J.L., Planchart A.;
RT "Mutations in Serac1 or Synj2 cause proximal t haplotype-mediated male
RT mouse sterility but not transmission ratio distortion.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3342-3347(2005).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U213-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U213-2; Sequence=VSP_022864;
CC Name=3;
CC IsoId=Q3U213-3; Sequence=VSP_022865, VSP_022866;
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:15722415}.
CC -!- SIMILARITY: Belongs to the SERAC1 family. {ECO:0000305}.
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DR EMBL; AK019677; BAB31833.1; -; mRNA.
DR EMBL; AK154605; BAE32707.1; -; mRNA.
DR EMBL; AK155571; BAE33329.1; -; mRNA.
DR EMBL; AK162246; BAE36813.1; -; mRNA.
DR EMBL; AK170498; BAE41837.1; -; mRNA.
DR EMBL; BC119594; AAI19595.1; -; mRNA.
DR EMBL; BC119595; AAI19596.1; -; mRNA.
DR CCDS; CCDS28366.1; -. [Q3U213-2]
DR CCDS; CCDS49933.1; -. [Q3U213-1]
DR RefSeq; NP_001104487.1; NM_001111017.1. [Q3U213-1]
DR RefSeq; NP_796285.2; NM_177311.4. [Q3U213-2]
DR AlphaFoldDB; Q3U213; -.
DR BioGRID; 236459; 3.
DR STRING; 10090.ENSMUSP00000095043; -.
DR ESTHER; mouse-srac1; PGAP1.
DR PhosphoSitePlus; Q3U213; -.
DR SwissPalm; Q3U213; -.
DR MaxQB; Q3U213; -.
DR PaxDb; Q3U213; -.
DR PeptideAtlas; Q3U213; -.
DR PRIDE; Q3U213; -.
DR ProteomicsDB; 257393; -. [Q3U213-1]
DR ProteomicsDB; 257394; -. [Q3U213-2]
DR ProteomicsDB; 257395; -. [Q3U213-3]
DR Antibodypedia; 20005; 103 antibodies from 21 providers.
DR DNASU; 321007; -.
DR Ensembl; ENSMUST00000024570; ENSMUSP00000024570; ENSMUSG00000015659. [Q3U213-2]
DR Ensembl; ENSMUST00000097432; ENSMUSP00000095043; ENSMUSG00000015659. [Q3U213-1]
DR GeneID; 321007; -.
DR KEGG; mmu:321007; -.
DR UCSC; uc008afy.2; mouse. [Q3U213-2]
DR UCSC; uc008afz.2; mouse. [Q3U213-1]
DR CTD; 84947; -.
DR MGI; MGI:2447813; Serac1.
DR VEuPathDB; HostDB:ENSMUSG00000015659; -.
DR eggNOG; KOG2029; Eukaryota.
DR GeneTree; ENSGT00390000003560; -.
DR HOGENOM; CLU_023317_1_0_1; -.
DR InParanoid; Q3U213; -.
DR OMA; RRTEYIY; -.
DR OrthoDB; 1311762at2759; -.
DR PhylomeDB; Q3U213; -.
DR TreeFam; TF319689; -.
DR BioGRID-ORCS; 321007; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Serac1; mouse.
DR PRO; PR:Q3U213; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3U213; protein.
DR Bgee; ENSMUSG00000015659; Expressed in embryonic brain and 239 other tissues.
DR Genevisible; Q3U213; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; ISO:MGI.
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 Alternative splicing; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Mitochondrion; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..654
FT /note="Protein SERAC1"
FT /id="PRO_0000274673"
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 89..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022864"
FT VAR_SEQ 341..342
FT /note="VS -> DR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022865"
FT VAR_SEQ 343..654
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022866"
FT VARIANT 4
FT /note="A -> V (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15722415,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 6
FT /note="Y -> F (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15722415,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 7
FT /note="C -> F (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15722415,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 25
FT /note="T -> M"
FT /evidence="ECO:0000269|PubMed:15722415"
FT VARIANT 64
FT /note="Q -> T (in strain: BALB/cByJ and C57BL/6J; requires
FT 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:15722415,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 518
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:15722415"
SQ SEQUENCE 654 AA; 73987 MW; D75EE0017C3B579F CRC64;
MSLAAYCVIC CRRIGSFAPR SKSRTPWRNI RNIIRFTGSL IVGGSLFITY EVLALKKSLM
LDTQVVEREK MKSYIYVHKA PVDRLDNRGI VWQARKELHR AVRKLLAAAA KVLRSPFADS
FSTVDIEDHD CAVWLLLRKS REDDLAARLQ AVREMSEAHH WHDYQYRIIA QACDPRTLIG
LARSKESDLR FFLPPPPLPS LKEDSSTEEE LRHLLASLPQ TELDECLQYF TSLALSESSQ
SLAAQKGGLW CFGGNGLPYA ESFGKVPSAT VEMFCLEAIV KHSEIPSHCD HIEAGGGLQL
LQRLYQLHKD CPKVQRNVMR IIGNMALNEH LHPAIVHSGW VSLMAEALKS SHIMEASHAA
RTLANLDRET VGEKYQDGVY VLHPQCRTSQ PIKADVLFIH GLMGAAFKTW RQHDSQRALT
ESAVVDEDRY TTCWPKTWLA KDCPSLRIIS VEYDTSLSDW RARCPMERKS IAFRSNELLS
KLRAAGVGDR PMIWISHSMG GLLVKKMLLE ASKKPELNAL INNTRGIIFY SVPHHGSRLA
EYSVNIRYLL FPSLEVKELS KDSPALKTLQ DDFLEFAKDK NFQVLNFVET QPTFIGSMIK
LHVVPVESAD LGIGDLIPVD VNHLNICKPK TKDAFLYQRT LQFICETLAR DLEN
