SERHL_MOUSE
ID SERHL_MOUSE Reviewed; 311 AA.
AC Q9EPB5; Q9DCZ8;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine hydrolase-like protein;
DE Short=SHL;
DE EC=3.1.-.-;
GN Name=Serhl;
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 [MRNA].
RC STRAIN=C57BL/10; TISSUE=Muscle;
RX PubMed=11352564; DOI=10.1006/geno.2000.6483;
RA Sadusky T.J., Kemp T.J., Simon M., Carey N., Coulton G.R.;
RT "Identification of Serhl, a new member of the serine hydrolase family
RT induced by passive stretch of skeletal muscle in vivo.";
RL Genomics 73:38-49(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable serine hydrolase. May be related to cell muscle
CC hypertrophy.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Peroxisome.
CC Note=Concentrated in perinuclear vesicles. May be located in
CC peroxisomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Serhl-1;
CC IsoId=Q9EPB5-1; Sequence=Displayed;
CC Name=Serhl-2; Synonyms=short;
CC IsoId=Q9EPB5-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Ubiquitous. High protein expression in skeletal and
CC cardiac muscle.
CC -!- DEVELOPMENTAL STAGE: Present in both unfused and recently fused
CC myotubes, but not thereafter.
CC -!- INDUCTION: Induced by passive stretch of skeletal muscle.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AJ251200; CAC20674.1; -; mRNA.
DR EMBL; AJ245737; CAC20673.1; -; mRNA.
DR EMBL; AK002313; BAB22007.1; -; mRNA.
DR EMBL; AK003827; BAB23023.1; -; mRNA.
DR EMBL; BC055431; AAH55431.1; -; mRNA.
DR CCDS; CCDS49682.1; -. [Q9EPB5-1]
DR RefSeq; NP_075964.1; NM_023475.3. [Q9EPB5-1]
DR AlphaFoldDB; Q9EPB5; -.
DR SMR; Q9EPB5; -.
DR STRING; 10090.ENSMUSP00000077345; -.
DR ChEMBL; CHEMBL3259500; -.
DR ESTHER; mouse-SERHL; SERHL.
DR MEROPS; S33.012; -.
DR iPTMnet; Q9EPB5; -.
DR PhosphoSitePlus; Q9EPB5; -.
DR EPD; Q9EPB5; -.
DR jPOST; Q9EPB5; -.
DR MaxQB; Q9EPB5; -.
DR PaxDb; Q9EPB5; -.
DR PRIDE; Q9EPB5; -.
DR ProteomicsDB; 261322; -. [Q9EPB5-1]
DR Antibodypedia; 45931; 62 antibodies from 12 providers.
DR DNASU; 68607; -.
DR Ensembl; ENSMUST00000078218; ENSMUSP00000077345; ENSMUSG00000058586. [Q9EPB5-1]
DR GeneID; 68607; -.
DR KEGG; mmu:68607; -.
DR UCSC; uc011zwz.1; mouse. [Q9EPB5-1]
DR CTD; 94009; -.
DR MGI; MGI:1890404; Serhl.
DR VEuPathDB; HostDB:ENSMUSG00000058586; -.
DR eggNOG; KOG1454; Eukaryota.
DR GeneTree; ENSGT00530000063960; -.
DR HOGENOM; CLU_020336_8_3_1; -.
DR InParanoid; Q9EPB5; -.
DR OMA; RGLMPVP; -.
DR PhylomeDB; Q9EPB5; -.
DR TreeFam; TF326547; -.
DR BioGRID-ORCS; 68607; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Serhl; mouse.
DR PRO; PR:Q9EPB5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9EPB5; protein.
DR Bgee; ENSMUSG00000058586; Expressed in ventricular system choroidal fissure and 230 other tissues.
DR ExpressionAtlas; Q9EPB5; baseline and differential.
DR Genevisible; Q9EPB5; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:MGI.
DR GO; GO:0016787; F:hydrolase activity; ISS:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..311
FT /note="Serine hydrolase-like protein"
FT /id="PRO_0000097693"
FT DOMAIN 27..227
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 102
FT /evidence="ECO:0000255"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 13
FT /note="W -> R (in Ref. 2; BAB22007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 35311 MW; 273404E85F07556E CRC64;
MGLHSELKLA VPWGHIALKV WGSQKNPPVL CLHGWLDNAN SFDRLIPLLP QDFCYMAMDF
GGHGLSSHYN PGLPYYQQNF VSEVRRVATA FKWNQFTLLG HSFGGCVGGT FACMFPEMVD
KLILLDSTPF FLDSNEMENI LTYRRRNIEH TLQVEASQKK SLRAVSPEEM LQGFLNNNSH
LDKDCGELIL QRGTTKVDAG LVLNRDRRIS WPENSFDFVS KEMFVHSAKS LQASVLMIKA
LQGYYDVRRA NDADKAPMHF MVDTLRSTLK ERFQFVEVPG NHYIHMNKPQ VVAGVVGPFL
QGLQRMTSAR L
