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Protein SERAC1 (Serine active site-containing protein 1)

 SRAC1_HUMAN             Reviewed;         654 AA.
Q96JX3; Q49AT1; Q5VTX3; Q6PKF3;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-APR-2018, entry version 129.
RecName: Full=Protein SERAC1;
AltName: Full=Serine active site-containing protein 1;
Name=SERAC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
THR-543.
TISSUE=Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INVOLVEMENT IN MEGDEL.
PubMed=23707711; DOI=10.1016/j.ymgme.2013.04.021;
Tort F., Garcia-Silva M.T., Ferrer-Cortes X., Navarro-Sastre A.,
Garcia-Villoria J., Coll M.J., Vidal E., Jimenez-Almazan J.,
Dopazo J., Briones P., Elpeleg O., Ribes A.;
"Exome sequencing identifies a new mutation in SERAC1 in a patient
with 3-methylglutaconic aciduria.";
Mol. Genet. Metab. 110:73-77(2013).
[5]
VARIANTS MEGDEL ASP-401; GLU-404; LEU-479 DEL AND THR-498, FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22683713; DOI=10.1038/ng.2325;
Wortmann S.B., Vaz F.M., Gardeitchik T., Vissers L.E., Renkema G.H.,
Schuurs-Hoeijmakers J.H., Kulik W., Lammens M., Christin C.,
Kluijtmans L.A., Rodenburg R.J., Nijtmans L.G., Grunewald A.,
Klein C., Gerhold J.M., Kozicz T., van Hasselt P.M., Harakalova M.,
Kloosterman W., Baric I., Pronicka E., Ucar S.K., Naess K.,
Singhal K.K., Krumina Z., Gilissen C., van Bokhoven H., Veltman J.A.,
Smeitink J.A., Lefeber D.J., Spelbrink J.N., Wevers R.A., Morava E.,
de Brouwer A.P.;
"Mutations in the phospholipid remodeling gene SERAC1 impair
mitochondrial function and intracellular cholesterol trafficking and
cause dystonia and deafness.";
Nat. Genet. 44:797-802(2012).
[6]
VARIANT MEGDEL GLU-526.
PubMed=28778788; DOI=10.1016/j.ejmg.2017.07.013;
Radha Rama Devi A., Lingappa L.;
"Novel mutations in SERAC1 gene in two Indian patients presenting with
dystonia and intellectual disability.";
Eur. J. Med. Genet. 61:100-103(2018).
-!- FUNCTION: Plays an important role in the phosphatidylglycerol
remodeling that is essential for both mitochondrial function and
intracellular cholesterol trafficking. May catalyze the remodeling
of phosphatidylglycerol and be involved in the transacylation-
acylation reaction to produce phosphatidylglycerol-36:1. May be
involved in bis(monoacylglycerol)phosphate biosynthetic pathway.
{ECO:0000269|PubMed:22683713}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}. Endoplasmic reticulum
{ECO:0000269|PubMed:22683713}. Mitochondrion
{ECO:0000269|PubMed:22683713}. Note=Localizes at the endoplasmic
reticulum and at the endoplasmic reticulum-mitochondria interface.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96JX3-1; Sequence=Displayed;
Name=2;
IsoId=Q96JX3-2; Sequence=VSP_022859, VSP_022860;
Name=3;
IsoId=Q96JX3-3; Sequence=VSP_022857, VSP_022858;
-!- TISSUE SPECIFICITY: Widely expressed, with predominant expression
in fetal skeletal muscle and adult brain. In the brain, highest
levels are found in the frontal and occipital cortices, cerebellum
and hippocampus. {ECO:0000269|PubMed:22683713}.
-!- DISEASE: 3-methylglutaconic aciduria with deafness,
encephalopathy, and Leigh-like syndrome (MEGDEL) [MIM:614739]: An
autosomal recessive disorder characterized by childhood onset of
delayed psychomotor development or psychomotor regression,
sensorineural deafness, spasticity or dystonia, and increased
excretion of 3-methylglutaconic acid. Brain imaging shows cerebral
and cerebellar atrophy as well as lesions in the basal ganglia
reminiscent of Leigh syndrome. Laboratory studies show increased
serum lactate and alanine, mitochondrial oxidative phosphorylation
defects, abnormal mitochondria, abnormal phosphatidylglycerol and
cardiolipin profiles in fibroblasts, and abnormal accumulation of
unesterified cholesterol within cells.
{ECO:0000269|PubMed:22683713, ECO:0000269|PubMed:23707711,
ECO:0000269|PubMed:28778788}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SERAC1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK027823; BAB55393.1; -; mRNA.
EMBL; AL135907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001705; AAH01705.1; -; mRNA.
EMBL; BC028594; AAH28594.1; -; mRNA.
CCDS; CCDS5255.1; -. [Q96JX3-1]
RefSeq; NP_116250.3; NM_032861.3. [Q96JX3-1]
UniGene; Hs.154706; -.
ProteinModelPortal; Q96JX3; -.
BioGrid; 124380; 6.
IntAct; Q96JX3; 2.
STRING; 9606.ENSP00000356071; -.
ESTHER; human-SERAC1; PGAP1.
iPTMnet; Q96JX3; -.
PhosphoSitePlus; Q96JX3; -.
BioMuta; SERAC1; -.
DMDM; 74751971; -.
EPD; Q96JX3; -.
MaxQB; Q96JX3; -.
PaxDb; Q96JX3; -.
PeptideAtlas; Q96JX3; -.
PRIDE; Q96JX3; -.
Ensembl; ENST00000367101; ENSP00000356068; ENSG00000122335. [Q96JX3-2]
Ensembl; ENST00000367104; ENSP00000356071; ENSG00000122335. [Q96JX3-1]
Ensembl; ENST00000607000; ENSP00000475788; ENSG00000122335. [Q96JX3-3]
GeneID; 84947; -.
KEGG; hsa:84947; -.
UCSC; uc003qrc.3; human. [Q96JX3-1]
CTD; 84947; -.
DisGeNET; 84947; -.
EuPathDB; HostDB:ENSG00000122335.13; -.
GeneCards; SERAC1; -.
HGNC; HGNC:21061; SERAC1.
HPA; HPA025715; -.
HPA; HPA025716; -.
MalaCards; SERAC1; -.
MIM; 614725; gene.
MIM; 614739; phenotype.
neXtProt; NX_Q96JX3; -.
OpenTargets; ENSG00000122335; -.
Orphanet; 352328; MEGDEL syndrome.
PharmGKB; PA134951844; -.
eggNOG; KOG2029; Eukaryota.
eggNOG; ENOG410YIPC; LUCA.
GeneTree; ENSGT00390000003560; -.
HOGENOM; HOG000154411; -.
HOVERGEN; HBG057428; -.
InParanoid; Q96JX3; -.
OMA; KTMANLD; -.
OrthoDB; EOG091G061M; -.
PhylomeDB; Q96JX3; -.
TreeFam; TF319689; -.
GeneWiki; SERAC1; -.
GenomeRNAi; 84947; -.
PRO; PR:Q96JX3; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000122335; -.
CleanEx; HS_SERAC1; -.
ExpressionAtlas; Q96JX3; baseline and differential.
Genevisible; Q96JX3; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0032367; P:intracellular cholesterol transport; IMP:UniProtKB.
GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; IMP:UniProtKB.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Deafness; Disease mutation;
Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
Mitochondrion; Phospholipid biosynthesis; Phospholipid metabolism;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 654 Protein SERAC1.
/FTId=PRO_0000274671.
TRANSMEM 32 54 Helical. {ECO:0000255}.
VAR_SEQ 163 167 DYQYR -> GNETT (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022857.
VAR_SEQ 168 654 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022858.
VAR_SEQ 469 531 KSIAFRSNELLRKLRAAGVGDRPVVWISHSMGGLLVKKMLL
EASTKPEMSTVINNTRGIIFYS -> RSLLSISSGIVEGLE
SPLHSEATNFLGSSELLVLGIGQWFGYHIAWEVFLSKRCCW
KPLRSQK (in isoform 2). {ECO:0000305}.
/FTId=VSP_022859.
VAR_SEQ 532 654 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_022860.
VARIANT 401 401 G -> D (in MEGDEL).
{ECO:0000269|PubMed:22683713}.
/FTId=VAR_068442.
VARIANT 404 404 G -> E (in MEGDEL).
{ECO:0000269|PubMed:22683713}.
/FTId=VAR_068443.
VARIANT 479 479 Missing (in MEGDEL).
{ECO:0000269|PubMed:22683713}.
/FTId=VAR_068444.
VARIANT 498 498 S -> T (in MEGDEL; dbSNP:rs201941476).
{ECO:0000269|PubMed:22683713}.
/FTId=VAR_068445.
VARIANT 526 526 G -> E (in MEGDEL; unknown pathological
significance).
{ECO:0000269|PubMed:28778788}.
/FTId=VAR_080230.
VARIANT 543 543 S -> T (in dbSNP:rs17849527).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030342.
CONFLICT 47 47 F -> L (in Ref. 3; AAH28594).
{ECO:0000305}.
SEQUENCE 654 AA; 74147 MW; B40F3B41C0FBEDDE CRC64;
MSLAAYCVIC CRRIGTSTSP PKSGTHWRDI RNIIKFTGSL ILGGSLFLTY EVLALKKAVT
LDTQVVEREK MKSYIYVHTV SLDKGENHGI AWQARKELHK AVRKVLATSA KILRNPFADP
FSTVDIEDHE CAVWLLLRKS KSDDKTTRLE AVREMSETHH WHDYQYRIIA QACDPKTLIG
LARSEESDLR FFLLPPPLPS LKEDSSTEEE LRQLLASLPQ TELDECIQYF TSLALSESSQ
SLAAQKGGLW CFGGNGLPYA ESFGEVPSAT VEMFCLEAIV KHSEISTHCD KIEANGGLQL
LQRLYRLHKD CPKVQRNIMR VIGNMALNEH LHSSIVRSGW VSIMAEAMKS PHIMESSHAA
RILANLDRET VQEKYQDGVY VLHPQYRTSQ PIKADVLFIH GLMGAAFKTW RQQDSEQAVI
EKPMEDEDRY TTCWPKTWLA KDCPALRIIS VEYDTSLSDW RARCPMERKS IAFRSNELLR
KLRAAGVGDR PVVWISHSMG GLLVKKMLLE ASTKPEMSTV INNTRGIIFY SVPHHGSRLA
EYSVNIRYLL FPSLEVKELS KDSPALKTLQ DDFLEFAKDK NFQVLNFVET LPTYIGSMIK
LHVVPVESAD LGIGDLIPVD VNHLNICKPK KKDAFLYQRT LQFIREALAK DLEN


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