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 14-OCT-2015, entry version 102. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION RP BY 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 RT 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 Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Ubiquitous. High protein expression in CC skeletal and 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. CC {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 UniGene; Mm.30056; -. DR ProteinModelPortal; Q9EPB5; -. DR SMR; Q9EPB5; 15-167. DR STRING; 10090.ENSMUSP00000077345; -. DR ChEMBL; CHEMBL3259500; -. DR ESTHER; mouse-SERHL; AlphaBeta_hydrolase. DR MEROPS; S33.012; -. DR PhosphoSite; Q9EPB5; -. DR MaxQB; Q9EPB5; -. DR PaxDb; Q9EPB5; -. DR PRIDE; Q9EPB5; -. 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 eggNOG; COG0596; -. DR GeneTree; ENSGT00530000063960; -. DR HOVERGEN; HBG023947; -. DR InParanoid; Q9EPB5; -. DR PhylomeDB; Q9EPB5; -. DR TreeFam; TF326547; -. DR NextBio; 327546; -. DR PRO; PR:Q9EPB5; -. DR Proteomes; UP000000589; Chromosome 15. DR Bgee; Q9EPB5; -. DR CleanEx; MM_SERHL; -. DR ExpressionAtlas; Q9EPB5; baseline and differential. DR Genevisible; Q9EPB5; MM. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA: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; IBA:GO_Central. 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; Complete proteome; Cytoplasm; Hydrolase; KW Peroxisome; Phosphoprotein; Reference proteome. FT CHAIN 1 311 Serine hydrolase-like protein. FT /FTId=PRO_0000097693. FT ACT_SITE 102 102 {ECO:0000255}. FT MOD_RES 210 210 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT CONFLICT 13 13 W -> R (in Ref. 2; BAB22007). FT {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 //