ID   Q5T6H7_HUMAN            Unreviewed;       552 AA.
AC   Q5T6H7;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   SubName: Full=X-prolyl aminopeptidase 1 {ECO:0000313|Ensembl:ENSP00000358697.1};
GN   Name=XPNPEP1 {ECO:0000313|Ensembl:ENSP00000358697.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000358697.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000358697.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [2] {ECO:0007829|PubMed:19608861}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [3] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [4] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [5] {ECO:0000313|Ensembl:ENSP00000358697.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|RuleBase:RU000590}.
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DR   EMBL; AL354951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001311057.1; NM_001324128.1.
DR   RefSeq; XP_016872103.1; XM_017016614.1.
DR   RefSeq; XP_016872104.1; XM_017016615.1.
DR   AlphaFoldDB; Q5T6H7; -.
DR   SMR; Q5T6H7; -.
DR   EPD; Q5T6H7; -.
DR   MassIVE; Q5T6H7; -.
DR   MaxQB; Q5T6H7; -.
DR   PeptideAtlas; Q5T6H7; -.
DR   ProteomicsDB; 64586; -.
DR   Antibodypedia; 31645; 222 antibodies from 34 providers.
DR   DNASU; 7511; -.
DR   Ensembl; ENST00000369683.5; ENSP00000358697.1; ENSG00000108039.18.
DR   GeneID; 7511; -.
DR   UCSC; uc001kyq.3; human.
DR   CTD; 7511; -.
DR   HGNC; HGNC:12822; XPNPEP1.
DR   VEuPathDB; HostDB:ENSG00000108039; -.
DR   GeneTree; ENSGT00940000157716; -.
DR   OrthoDB; 869at2759; -.
DR   BioGRID-ORCS; 7511; 25 hits in 1166 CRISPR screens.
DR   ChiTaRS; XPNPEP1; human.
DR   GenomeRNAi; 7511; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000108039; Expressed in body of pancreas and 207 other cell types or tissues.
DR   ExpressionAtlas; Q5T6H7; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590};
KW   Proteomics identification {ECO:0007829|EPD:Q5T6H7,
KW   ECO:0007829|MaxQB:Q5T6H7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          257..471
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          486..548
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   552 AA;  62139 MW;  627539255505E5CE CRC64;
     MWTDGRYFLQ AAKQMDSNWT LMKMGLKDTP TQEDWLVSVL PEGSRVGVDP LIIPTDYWKK
     MAKVLRSAGH HLIPVKENLV DKIWTDRPER PCKPLLTLGL DYTGISWKDK VADLRLKMAE
     RNVMWFVVTA LDEIAWLFNL RGSDVEHNPV FFSYAIIGLE TIMLFIDGDR IDAPSVKEHL
     LLDLGLEAEY RIQVHPYKSI LSELKALCAD LSPREKVWVS DKASYAVSET IPKDHRCCMP
     YTPICIAKAV KNSAESEGMR RAHIKDAVAL CELFNWLEKE VPKGGVTEIS AADKAEEFRR
     QQADFVDLSF PTISSTGPNG AIIHYAPVPE TNRTLSLDEV YLIDSGAQYK DGTTDVTRTM
     HFGTPTAYEK ECFTYVLKGH IAVSAAVFPT GTKGHLLDSF ARSALWDSGL DYLHGTGHGV
     GSFLNVHEGP CGISYKTFSD EPLEAGMIVT DEPGYYEDGA FGIRIENVVL VVPVKTKYNF
     NNRGSLTFEP LTLVPIQTKM IDVDSLTDKE CDWLNNYHLT CRDVIGKELQ KQGRQEALEW
     LIRETQPISK QH
//