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PSA_MOUSE
ID   PSA_MOUSE               Reviewed;         920 AA.
AC   Q11011; Q3UZE0; Q5PR74; Q91VJ8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Puromycin-sensitive aminopeptidase;
DE            Short=PSA;
DE            EC=3.4.11.14;
DE   AltName: Full=Cytosol alanyl aminopeptidase;
DE            Short=AAP-S;
GN   Name=Npepps; Synonyms=Psa;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=7592939; DOI=10.1074/jbc.270.45.26931;
RA   Constam D.B., Tobler A.R., Rensing-Ehl A., Kemler I., Hersh L.B.,
RA   Fontana A.;
RT   "Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and
RT   functional characterization.";
RL   J. Biol. Chem. 270:26931-26939(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-920.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [6]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=10407043; DOI=10.1523/jneurosci.19-14-06068.1999;
RA   Osada T., Ikegami S., Takiguchi-Hayashi K., Yamazaki Y., Katoh-Fukui Y.,
RA   Higashinakagawa T., Sakaki Y., Takeuchi T.;
RT   "Increased anxiety and impaired pain response in puromycin-sensitive
RT   aminopeptidase gene-deficient mice obtained by a mouse gene-trap method.";
RL   J. Neurosci. 19:6068-6078(1999).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11376108; DOI=10.1210/mend.15.6.0644;
RA   Osada T., Watanabe G., Sakaki Y., Takeuchi T.;
RT   "Puromycin-sensitive aminopeptidase is essential for the maternal
RT   recognition of pregnancy in mice.";
RL   Mol. Endocrinol. 15:882-893(2001).
RN   [8]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=11376114; DOI=10.1210/mend.15.6.0643;
RA   Osada T., Watanabe G., Kondo S., Toyoda M., Sakaki Y., Takeuchi T.;
RT   "Male reproductive defects caused by puromycin-sensitive aminopeptidase
RT   deficiency in mice.";
RL   Mol. Endocrinol. 15:960-971(2001).
RN   [9]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-465, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA   Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA   Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT   disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18209067; DOI=10.4049/jimmunol.180.3.1704;
RA   Towne C.F., York I.A., Neijssen J., Karow M.L., Murphy A.J.,
RA   Valenzuela D.M., Yancopoulos G.D., Neefjes J.J., Rock K.L.;
RT   "Puromycin-sensitive aminopeptidase limits MHC class I presentation in
RT   dendritic cells but does not affect CD8 T cell responses during viral
RT   infections.";
RL   J. Immunol. 180:1704-1712(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, 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 expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Aminopeptidase with broad substrate specificity for several
CC       peptides. Involved in proteolytic events essential for cell growth and
CC       viability. May act as regulator of neuropeptide activity. Plays a role
CC       in the antigen-processing pathway for MHC class I molecules. Involved
CC       in the N-terminal trimming of cytotoxic T-cell epitope precursors.
CC       Digests the poly-Q peptides found in many cellular proteins.
CC       {ECO:0000269|PubMed:7592939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, preferentially alanine,
CC         from a wide range of peptides, amides and arylamides.; EC=3.4.11.14;
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: Strongly inhibited by bestatin, leuhistin,
CC       actinonin, amastatin, 1,10-phenanthroline, DFP, PCMBS, Zn(2+), Cd(2+),
CC       Co(2+), Cu(2+), Hg(2+), EDTA and puromycin. Not inhibited by PMSF, and
CC       only slightly inhibited by leupeptin and aprotinin. Activity is
CC       increased by Mg(2+) and Ca(2+) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7592939}.
CC       Nucleus {ECO:0000269|PubMed:7592939}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain,
CC       particularly the striatum and hippocampus. Expressed in Sertoli cells.
CC       {ECO:0000269|PubMed:10407043, ECO:0000269|PubMed:11376114,
CC       ECO:0000269|PubMed:7592939}.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit dwarfism, increased anxiety,
CC       impaired pain responses and do not reproduce as well as wild-type mice.
CC       More MHC class I molecules are displayed on dendritic cell surfaces.
CC       {ECO:0000269|PubMed:10407043, ECO:0000269|PubMed:11376108,
CC       ECO:0000269|PubMed:11376114, ECO:0000269|PubMed:18209067}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-46 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; U35646; AAC52409.1; -; mRNA.
DR   EMBL; AL627445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466556; EDL16075.1; -; Genomic_DNA.
DR   EMBL; BC009653; AAH09653.1; -; mRNA.
DR   EMBL; BC086798; AAH86798.1; -; mRNA.
DR   EMBL; BC098212; AAH98212.1; -; mRNA.
DR   EMBL; AK133898; BAE21917.1; -; mRNA.
DR   CCDS; CCDS25317.1; -.
DR   PIR; T10052; T10052.
DR   RefSeq; NP_032968.2; NM_008942.2.
DR   AlphaFoldDB; Q11011; -.
DR   SMR; Q11011; -.
DR   BioGRID; 202409; 21.
DR   IntAct; Q11011; 5.
DR   MINT; Q11011; -.
DR   STRING; 10090.ENSMUSP00000001480; -.
DR   MEROPS; M01.010; -.
DR   iPTMnet; Q11011; -.
DR   PhosphoSitePlus; Q11011; -.
DR   SwissPalm; Q11011; -.
DR   EPD; Q11011; -.
DR   jPOST; Q11011; -.
DR   MaxQB; Q11011; -.
DR   PaxDb; Q11011; -.
DR   PeptideAtlas; Q11011; -.
DR   PRIDE; Q11011; -.
DR   ProteomicsDB; 291537; -.
DR   Antibodypedia; 8552; 280 antibodies from 28 providers.
DR   DNASU; 19155; -.
DR   Ensembl; ENSMUST00000001480; ENSMUSP00000001480; ENSMUSG00000001441.
DR   GeneID; 19155; -.
DR   KEGG; mmu:19155; -.
DR   UCSC; uc007ldv.2; mouse.
DR   CTD; 9520; -.
DR   MGI; MGI:1101358; Npepps.
DR   VEuPathDB; HostDB:ENSMUSG00000001441; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   GeneTree; ENSGT00940000155246; -.
DR   InParanoid; Q11011; -.
DR   OMA; MMEYVAI; -.
DR   OrthoDB; 110058at2759; -.
DR   PhylomeDB; Q11011; -.
DR   TreeFam; TF300395; -.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 19155; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Npepps; mouse.
DR   PRO; PR:Q11011; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q11011; protein.
DR   Bgee; ENSMUSG00000001441; Expressed in rostral migratory stream and 272 other tissues.
DR   ExpressionAtlas; Q11011; baseline and differential.
DR   Genevisible; Q11011; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; ISO:MGI.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
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   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Nitration; Nucleus; Protease; Reference proteome; Zinc.
FT   CHAIN           1..920
FT                   /note="Puromycin-sensitive aminopeptidase"
FT                   /id="PRO_0000095117"
FT   MOTIF           727..731
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         317..321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            439
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         465
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16800626"
FT   CONFLICT        185
FT                   /note="A -> P (in Ref. 1; AAC52409)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   920 AA;  103325 MW;  BECF4139F074A356 CRC64;
     MWLAAAVPSL ARRLLLLGPP PPPLLLLLSR SSRRRRRLHS LGLAAMPEKR PFERLPAEVS
     PINYSLCLKP DLLDFTFEGK LEAAAQVRQA TNQIVMNCAD IDIITASYAP EGDEEIHATG
     FNYQNEDEKV TLSFPSTLQT GTGTLKIDFV GELNDKMKGF YRSRYTTPAG EVRYAAVTQF
     EATDARRAFP CWDEPAIKAT FDISLVVPKD RVALSNMNVI DRKPYPDDEN LVEVKFARTP
     VMSTYLVAFV VGEYDFVETR SKDGVCVRVY TPVGKAEQGK FALEVAAKTL PFYKDYFNVP
     YPLPKIDLIA IADFAAGAME NWGLVTYRET ALLIDPKNSC SSSRQWVALV VGHELAHQWF
     GNLVTMEWWT HLWLNEGFAS WIEYLCVDHC FPEYDIWTQF VSADYTRAQE LDALDNSHPI
     EVSVGHPSEV DEIFDAISYS KGASVIRMLH DYIGDKDFKK GMNMYLTKFQ QKNAATEDLW
     ESLESASGKP IAAVMNTWTK QMGFPLIYVE AEQVEDDRVL KLSQKKFCAS GPYGGEDCPQ
     WMVPITISTS EDPNQAKLKI LMDKPEMSVV LKNVKPDQWV KLNLGTVGFY RTQYSSAMLE
     SLLPGIRDLS LPPVDRLGLQ NDLFSLARAG IISTVEVLKV MEAFVNEPNY TVWSDLSCNL
     GILSTLLSHT DFYEEIQEFV KDVFSPIGER LGWDPKPGEG HLDALLRGLV LGKLGKAGHK
     ATLEEARRRF KEHVEGKQIL SADLRSPVYL TVLKHGDGAT LDIMLKLHKQ ADMQEEKNRI
     ERVLGATLSP ELIQKVLTFA LSEEVRPQDT VSVIGGVAGG SKHGRKAAWK FIKDNWEELH
     NRYQGGFLIS RLIKLSVEGF AVDKMAGEVK AFFESHPAPS AERTIQQCCE NILLNAAWLK
     RDADSIHQYL LQRKTSPPSV
 
 
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