ID SERHL_MOUSE STANDARD; PRT; 311 AA. AC Q9EPB5; Q9DCZ8; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Serine hydrolase-like protein (EC 3.1.-.-) (SHL). 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/10; TISSUE=Muscle; RX MEDLINE=21251001; 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 Schonbach 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Probable serine hydrolase. May be related to cell muscle CC hypertrophy. CC -!- SUBCELLULAR LOCATION: Cytoplasmic; concentrated in perinuclear CC vesicles. May be located in 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 --------------------------------------------------------------------------- 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 MEROPS; S33.012; -. DR Ensembl; ENSMUSG00000058586; Mus musculus. DR MGI; MGI:1890404; Serhl. DR GO; GO:0016023; C:cytoplasmic membrane-bound vesicle; IDA. DR InterPro; IPR000073; A/b_hydrolase. DR InterPro; IPR003089; AB_hydrolase. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00111; ABHYDROLASE. KW Alternative splicing; Hydrolase. FT ACT_SITE 102 102 Probable. FT CONFLICT 13 13 W -> R (in Ref. 2; BAB22007). 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 //