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Puromycin-sensitive aminopeptidase (PSA) (EC 3.4.11.14) (Cytosol alanyl aminopeptidase) (AAP-S)

 PSA_MOUSE               Reviewed;         920 AA.
Q11011; Q3UZE0; Q5PR74; Q91VJ8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 2.
07-JUN-2017, entry version 154.
RecName: Full=Puromycin-sensitive aminopeptidase;
Short=PSA;
EC=3.4.11.14;
AltName: Full=Cytosol alanyl aminopeptidase;
Short=AAP-S;
Name=Npepps; Synonyms=Psa;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=7592939; DOI=10.1074/jbc.270.45.26931;
Constam D.B., Tobler A.R., Rensing-Ehl A., Kemler I., Hersh L.B.,
Fontana A.;
"Puromycin-sensitive aminopeptidase. Sequence analysis, expression,
and functional characterization.";
J. Biol. Chem. 270:26931-26939(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-920.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=10407043;
Osada T., Ikegami S., Takiguchi-Hayashi K., Yamazaki Y.,
Katoh-Fukui Y., Higashinakagawa T., Sakaki Y., Takeuchi T.;
"Increased anxiety and impaired pain response in puromycin-sensitive
aminopeptidase gene-deficient mice obtained by a mouse gene-trap
method.";
J. Neurosci. 19:6068-6078(1999).
[7]
DISRUPTION PHENOTYPE.
PubMed=11376108; DOI=10.1210/mend.15.6.0644;
Osada T., Watanabe G., Sakaki Y., Takeuchi T.;
"Puromycin-sensitive aminopeptidase is essential for the maternal
recognition of pregnancy in mice.";
Mol. Endocrinol. 15:882-893(2001).
[8]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=11376114; DOI=10.1210/mend.15.6.0643;
Osada T., Watanabe G., Kondo S., Toyoda M., Sakaki Y., Takeuchi T.;
"Male reproductive defects caused by puromycin-sensitive
aminopeptidase deficiency in mice.";
Mol. Endocrinol. 15:960-971(2001).
[9]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-465, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
Squier T.C., Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to
neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[10]
DISRUPTION PHENOTYPE.
PubMed=18209067; DOI=10.4049/jimmunol.180.3.1704;
Towne C.F., York I.A., Neijssen J., Karow M.L., Murphy A.J.,
Valenzuela D.M., Yancopoulos G.D., Neefjes J.J., Rock K.L.;
"Puromycin-sensitive aminopeptidase limits MHC class I presentation in
dendritic cells but does not affect CD8 T cell responses during viral
infections.";
J. Immunol. 180:1704-1712(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Aminopeptidase with broad substrate specificity for
several peptides. Involved in proteolytic events essential for
cell growth and viability. May act as regulator of neuropeptide
activity. Plays a role in the antigen-processing pathway for MHC
class I molecules. Involved in the N-terminal trimming of
cytotoxic T-cell epitope precursors. Digests the poly-Q peptides
found in many cellular proteins. {ECO:0000269|PubMed:7592939}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
preferentially alanine, from a wide range of peptides, amides and
arylamides.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Strongly inhibited by bestatin, leuhistin,
actinonin, amastatin, 1,10-phenanthroline, DFP, PCMBS, Zn(2+),
Cd(2+), Co(2+), Cu(2+), Hg(2+), EDTA and puromycin. Not inhibited
by PMSF, and only slightly inhibited by leupeptin and aprotinin.
Activity is increased by Mg(2+) and Ca(2+) (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:7592939}. Nucleus
{ECO:0000269|PubMed:7592939}.
-!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain,
particularly the striatum and hippocampus. Expressed in Sertoli
cells. {ECO:0000269|PubMed:10407043, ECO:0000269|PubMed:11376114,
ECO:0000269|PubMed:7592939}.
-!- DISRUPTION PHENOTYPE: Mice exhibit dwarfism, increased anxiety,
impaired pain responses and do not reproduce as well as wild-type
mice. More MHC class I molecules are displayed on dendritic cell
surfaces. {ECO:0000269|PubMed:10407043,
ECO:0000269|PubMed:11376108, ECO:0000269|PubMed:11376114,
ECO:0000269|PubMed:18209067}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-46 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U35646; AAC52409.1; -; mRNA.
EMBL; AL627445; CAM26998.1; -; Genomic_DNA.
EMBL; CH466556; EDL16075.1; -; Genomic_DNA.
EMBL; BC009653; AAH09653.1; -; mRNA.
EMBL; BC086798; AAH86798.1; -; mRNA.
EMBL; BC098212; AAH98212.1; -; mRNA.
EMBL; AK133898; BAE21917.1; -; mRNA.
CCDS; CCDS25317.1; -.
PIR; T10052; T10052.
RefSeq; NP_032968.2; NM_008942.2.
UniGene; Mm.29824; -.
ProteinModelPortal; Q11011; -.
SMR; Q11011; -.
IntAct; Q11011; 2.
MINT; MINT-4108858; -.
STRING; 10090.ENSMUSP00000001480; -.
MEROPS; M01.010; -.
iPTMnet; Q11011; -.
PhosphoSitePlus; Q11011; -.
SwissPalm; Q11011; -.
EPD; Q11011; -.
MaxQB; Q11011; -.
PaxDb; Q11011; -.
PeptideAtlas; Q11011; -.
PRIDE; Q11011; -.
Ensembl; ENSMUST00000001480; ENSMUSP00000001480; ENSMUSG00000001441.
GeneID; 19155; -.
KEGG; mmu:19155; -.
UCSC; uc007ldv.2; mouse.
CTD; 9520; -.
MGI; MGI:1101358; Npepps.
eggNOG; KOG1046; Eukaryota.
eggNOG; COG0308; LUCA.
GeneTree; ENSGT00760000119082; -.
HOGENOM; HOG000106482; -.
HOVERGEN; HBG106325; -.
InParanoid; Q11011; -.
KO; K08776; -.
OMA; YLTRHQY; -.
OrthoDB; EOG091G01GH; -.
PhylomeDB; Q11011; -.
TreeFam; TF300395; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; Npepps; mouse.
PRO; PR:Q11011; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000001441; -.
CleanEx; MM_NPEPPS; -.
ExpressionAtlas; Q11011; baseline and differential.
Genevisible; Q11011; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004177; F:aminopeptidase activity; ISO:MGI.
GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
GO; GO:0042277; F:peptide binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
CDD; cd09601; M1_APN_2; 1.
InterPro; IPR024571; ERAP1-like_C_dom.
InterPro; IPR034016; M1_APN-typ.
InterPro; IPR001930; Peptidase_M1.
InterPro; IPR014782; Peptidase_M1_N.
PANTHER; PTHR11533; PTHR11533; 1.
Pfam; PF11838; ERAP1_C; 1.
Pfam; PF01433; Peptidase_M1; 1.
PRINTS; PR00756; ALADIPTASE.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Metalloprotease; Nitration; Nucleus; Protease;
Reference proteome; Zinc.
CHAIN 1 920 Puromycin-sensitive aminopeptidase.
/FTId=PRO_0000095117.
REGION 317 321 Substrate binding. {ECO:0000250}.
MOTIF 727 731 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 354 354 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 353 353 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 357 357 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 376 376 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
BINDING 181 181 Substrate. {ECO:0000250}.
SITE 439 439 Transition state stabilizer.
{ECO:0000250}.
MOD_RES 465 465 Nitrated tyrosine.
{ECO:0000244|PubMed:16800626}.
CONFLICT 185 185 A -> P (in Ref. 1; AAC52409).
{ECO:0000305}.
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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