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 29-MAY-2024, entry version 100. DE RecName: Full=Aminopeptidase Q {ECO:0000305}; DE Short=AP-Q {ECO:0000305}; DE Short=APQ {ECO:0000250|UniProtKB:Q6Q4G3}; DE EC=3.4.11.- {ECO:0000250|UniProtKB:Q6Q4G3}; DE AltName: Full=Laeverin {ECO:0000250|UniProtKB:Q6Q4G3}; GN Name=Lvrn {ECO:0000312|MGI:MGI:1921824}; GN Synonyms=Aqpep {ECO:0000312|MGI:MGI:1921824}; 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 [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., 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 [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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Pancreas; 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: Metalloprotease which may be important for placentation by CC regulating biological activity of key peptides at the embryo-maternal CC interface. On synthetic substrates it shows a marked preference for CC Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys- CC LCA. Cleaves the N-terminal amino acid of several peptides such as CC angiotensin-3, kisspeptin-10 and endokinin C. CC {ECO:0000250|UniProtKB:Q6Q4G3}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited by bestatin. CC {ECO:0000250|UniProtKB:Q6Q4G3}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6Q4G3}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single- CC pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6Q4G3}. CC -!- SIMILARITY: Belongs to the peptidase M1 family. {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; AK014652; BAB29490.1; -; mRNA. DR EMBL; BC113158; AAI13159.1; -; mRNA. DR AlphaFoldDB; Q2KHK3; -. DR SMR; Q2KHK3; -. DR STRING; 10090.ENSMUSP00000025358; -. DR MEROPS; M01.026; -. DR GlyCosmos; Q2KHK3; 5 sites, No reported glycans. DR GlyGen; Q2KHK3; 5 sites. DR PhosphoSitePlus; Q2KHK3; -. DR PaxDb; 10090-ENSMUSP00000025358; -. DR ProteomicsDB; 281975; -. DR UCSC; uc008evx.1; mouse. DR AGR; MGI:1921824; -. DR MGI; MGI:1921824; Lvrn. DR eggNOG; KOG1046; Eukaryota. DR InParanoid; Q2KHK3; -. DR PhylomeDB; Q2KHK3; -. DR ChiTaRS; Lvrn; mouse. DR PRO; PR:Q2KHK3; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q2KHK3; Protein. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter. DR GO; GO:0042277; F:peptide binding; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd09601; M1_APN-Q_like; 1. DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1. DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1. DR InterPro; IPR045357; Aminopeptidase_N-like_N. DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf. DR InterPro; IPR034016; M1_APN-typ. DR InterPro; IPR001930; Peptidase_M1. DR InterPro; IPR014782; Peptidase_M1_dom. DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf. DR PANTHER; PTHR11533:SF31; AMINOPEPTIDASE Q; 1. DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1. DR Pfam; PF01433; Peptidase_M1; 1. DR Pfam; PF17900; Peptidase_M1_N; 1. DR PRINTS; PR00756; ALADIPTASE. DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1..559 FT /note="Aminopeptidase Q" FT /id="PRO_0000247069" FT TOPO_DOM 1..13 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q6Q4G3" FT TRANSMEM 14..34 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 35..559 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:Q6Q4G3" FT ACT_SITE 413 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 376..380 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 412 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 435 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT SITE 501 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT CARBOHYD 121 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 129 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 258 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 343 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 335 FT /note="N -> S (in Ref. 1; BAB29490)" FT /evidence="ECO:0000305" 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 //