ID AMPQ_MOUSE Reviewed; 559 AA. AC Q2KHK3; Q9D633; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 06-MAR-2013, entry version 51. DE RecName: Full=Aminopeptidase Q; DE Short=AP-Q; DE EC=3.4.11.-; DE AltName: Full=Laeverin; GN Name=Aqpep; Synonyms=Lvrn; 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 [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 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). CC -!- FUNCTION: Metalloprotease which may be important for placentation CC by regulating biological activity of key peptides at the embryo- CC maternal interface. On synthetic substrates it shows a marked CC preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- CC MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of CC several peptides such as angiotensin-3, kisspeptin-10 and CC endokinin C (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- ENZYME REGULATION: Inhibited by bestatin (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (By similarity). CC -!- PTM: N-glycosylated (By similarity). 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 IPI; IPI00674877; -. DR UniGene; Mm.26379; -. DR ProteinModelPortal; Q2KHK3; -. DR SMR; Q2KHK3; 86-551. DR STRING; Q2KHK3; -. DR MEROPS; M01.026; -. DR PhosphoSite; Q2KHK3; -. DR PaxDb; Q2KHK3; -. DR PRIDE; Q2KHK3; -. DR UCSC; uc008evx.1; mouse. DR MGI; MGI:1921824; 4833403I15Rik. DR eggNOG; COG0308; -. DR HOGENOM; HOG000106482; -. DR InParanoid; Q2KHK3; -. DR OrthoDB; EOG43R3KX; -. DR CleanEx; MM_4833403I15RIK; -. DR Genevestigator; Q2KHK3; -. DR GermOnline; ENSMUSG00000024481; Mus musculus. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_N. DR PANTHER; PTHR11533; PTHR11533; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR PRINTS; PR00756; ALADIPTASE. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 2: Evidence at transcript level; KW Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Protease; Reference proteome; Signal-anchor; KW Transmembrane; Transmembrane helix; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 559 Aminopeptidase Q. FT /FTId=PRO_0000247069. FT TOPO_DOM 2 13 Cytoplasmic (Potential). FT TRANSMEM 14 34 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 35 559 Lumenal (Potential). FT REGION 376 380 Substrate binding (By similarity). FT ACT_SITE 413 413 Proton acceptor (By similarity). FT METAL 412 412 Zinc; catalytic (By similarity). FT METAL 416 416 Zinc; catalytic (By similarity). FT METAL 435 435 Zinc; catalytic (By similarity). FT BINDING 237 237 Substrate (By similarity). FT SITE 501 501 Transition state stabilizer (By FT similarity). FT CARBOHYD 121 121 N-linked (GlcNAc...) (Potential). FT CARBOHYD 129 129 N-linked (GlcNAc...) (Potential). FT CARBOHYD 258 258 N-linked (GlcNAc...) (Potential). FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential). FT CARBOHYD 343 343 N-linked (GlcNAc...) (Potential). FT CONFLICT 335 335 N -> S (in Ref. 1; BAB29490). SQ SEQUENCE 559 AA; 63338 MW; 8C1FF55A36AE05F3 CRC64; MSRPFSSGVY VSRGVALLLA ALTAVLLLVL VALASLYGSC AHVQPSEQGN SRVKNTSLWP PGGQEWALPT PAQEPTVGTS QDLGPPSGPW DHLRLPPWLV PLHYDLELWP WLQPDKLSPP NLTFTGRVNI TVRCTVASSR LLLHSFLLNY KQVEVWGPLA QDTRNATVGR VQVEKVWFAP DMQFVVLDLG QSLEPGSRYE LSFHFSGQVL QVGLEGLFLN LYHDEDELRA LVATQMEPTF ARHVFPCFDE PALKATFNIT VIHHPGYAAL SNMPQLGQSE RIDVNGSRWT VTTFHTTPRM PTYLVALVVC DLDHISRTER GKEIRVWARK DDIANGYLDF AANITGPIFS FLEDLFNISY RLPKTDIVAL PIFASGAMEN WGLLIFDESS LLLEPEDELT EKRAMILSII AHEVGHQWFG NLVTMSWWNN IWLNEGFASY FELELTNYFY PKVPMNMIFF FTVLHGILGE DHALESRAVS TAVENFTETS EINRLFDLYT YKKGACMAWM LASFLSPHLF INALKSYLET FSYSNAEQDD LWRHIQMVIV PFRHFLAEH //