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 24-JAN-2024, entry version 141. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000077345; -. DR ProteomicsDB; 261322; -. [Q9EPB5-1] DR Pumba; Q9EPB5; -. DR Antibodypedia; 45931; 85 antibodies from 13 providers. DR DNASU; 68607; -. DR Ensembl; ENSMUST00000078218.11; ENSMUSP00000077345.5; ENSMUSG00000058586.13. [Q9EPB5-1] DR GeneID; 68607; -. DR KEGG; mmu:68607; -. DR UCSC; uc011zwz.1; mouse. [Q9EPB5-1] DR AGR; MGI:1890404; -. 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 OrthoDB; 35949at2759; -. DR PhylomeDB; Q9EPB5; -. DR TreeFam; TF326547; -. DR BioGRID-ORCS; 68607; 5 hits in 77 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 232 other cell types or 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; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1. DR PANTHER; PTHR43798:SF14; SERINE HYDROLASE-LIKE PROTEIN DDB_G0286239; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00111; ABHYDROLASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 //