ID LAEVR_MOUSE STANDARD; PRT; 558 AA. AC Q2KHK3; Q9D633; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 05-SEP-2006, entry version 6. DE Laeverin (EC 3.4.-.-). GN Name=Lvrn; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 metalloprotease, which may be involved in CC extravillous trophoblasts function (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; single-pass type II membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the peptidase M1 family. 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; AK014652; BAB29490.1; -; mRNA. DR EMBL; BC113158; AAI13159.1; -; mRNA. DR UniGene; Mm.26379; -. DR MEROPS; M01.026; -. DR MGI; MGI:1921824; 4833403I15Rik. DR ArrayExpress; Q2KHK3; -. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR001930; Peptidase_M1. DR PANTHER; PTHR11533; Peptidase_M1; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR PROSITE; PS00142; ZINC_PROTEASE; 1. KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; KW Protease; Signal-anchor; Transmembrane; Zinc. FT INIT_MET 0 0 By similarity. FT CHAIN 1 558 Laeverin. FT /FTId=PRO_0000247069. FT TOPO_DOM 1 12 Cytoplasmic (Potential). FT TRANSMEM 13 33 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 34 558 Lumenal (Potential). FT ACT_SITE 412 412 By similarity. FT ACT_SITE 500 500 Proton donor (Potential). FT METAL 411 411 Zinc (catalytic) (By similarity). FT METAL 415 415 Zinc (catalytic) (By similarity). FT METAL 434 434 Zinc (catalytic) (By similarity). FT CARBOHYD 120 120 N-linked (GlcNAc...) (Potential). FT CARBOHYD 128 128 N-linked (GlcNAc...) (Potential). FT CARBOHYD 257 257 N-linked (GlcNAc...) (Potential). FT CARBOHYD 284 284 N-linked (GlcNAc...) (Potential). FT CARBOHYD 342 342 N-linked (GlcNAc...) (Potential). FT CONFLICT 334 334 N -> S (in Ref. 1; BAB29490). SQ SEQUENCE 558 AA; 63206 MW; E2E121E206AE1F91 CRC64; SRPFSSGVYV SRGVALLLAA LTAVLLLVLV ALASLYGSCA HVQPSEQGNS RVKNTSLWPP GGQEWALPTP AQEPTVGTSQ DLGPPSGPWD HLRLPPWLVP LHYDLELWPW LQPDKLSPPN LTFTGRVNIT VRCTVASSRL LLHSFLLNYK QVEVWGPLAQ DTRNATVGRV QVEKVWFAPD MQFVVLDLGQ SLEPGSRYEL SFHFSGQVLQ VGLEGLFLNL YHDEDELRAL VATQMEPTFA RHVFPCFDEP ALKATFNITV IHHPGYAALS NMPQLGQSER IDVNGSRWTV TTFHTTPRMP TYLVALVVCD LDHISRTERG KEIRVWARKD DIANGYLDFA ANITGPIFSF LEDLFNISYR LPKTDIVALP IFASGAMENW GLLIFDESSL LLEPEDELTE KRAMILSIIA HEVGHQWFGN LVTMSWWNNI WLNEGFASYF ELELTNYFYP KVPMNMIFFF TVLHGILGED HALESRAVST AVENFTETSE INRLFDLYTY KKGACMAWML ASFLSPHLFI NALKSYLETF SYSNAEQDDL WRHIQMVIVP FRHFLAEH //