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P42785 (PCP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal Pro-X carboxypeptidase

EC=3.4.16.2
Alternative name(s):
Angiotensinase C
Lysosomal carboxypeptidase C
Proline carboxypeptidase
Prolylcarboxypeptidase
Short name=PRCP
Gene names
Name:PRCP
Synonyms:PCP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

Catalytic activity

Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.

Subunit structure

Homodimer. Ref.11

Subcellular location

Lysosome.

Tissue specificity

Highest levels in placenta, lung and liver. Also present in heart, brain, pancreas and kidney.

Sequence similarities

Belongs to the peptidase S28 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GPR37L1O608832EBI-2803892,EBI-2927498

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42785-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P42785-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-56: K → KALAAGQLHICIIQLNHYKTPL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 4524
PRO_0000027308
Chain46 – 496451Lysosomal Pro-X carboxypeptidase
PRO_0000027309

Regions

Region194 – 334141SKS domain

Sites

Active site1791Charge relay system Ref.11
Active site4301Charge relay system Ref.11
Active site4551Charge relay system Ref.11

Amino acid modifications

Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Ref.11
Glycosylation3171N-linked (GlcNAc...) Ref.9 Ref.11
Glycosylation3361N-linked (GlcNAc...) Ref.11
Glycosylation3451N-linked (GlcNAc...) Ref.11
Glycosylation4151N-linked (GlcNAc...) Ref.9 Ref.11
Disulfide bond215 ↔ 372 Ref.11
Disulfide bond233 ↔ 310 Ref.11
Disulfide bond264 ↔ 343 Ref.11
Disulfide bond364 ↔ 394 Ref.11

Natural variations

Alternative sequence561K → KALAAGQLHICIIQLNHYKT PL in isoform 2.
VSP_045799
Natural variant1121E → D. Ref.3
Corresponds to variant rs2298668 [ dbSNP | Ensembl ].
VAR_020464
Natural variant4441T → S.
Corresponds to variant rs2228312 [ dbSNP | Ensembl ].
VAR_029329

Experimental info

Sequence conflict1041G → E in BAG52417. Ref.3
Sequence conflict2481S → L in BAG52417. Ref.3
Sequence conflict3041W → R in BAG52417. Ref.3

Secondary structure

................................................................... 496
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FC5DD570D3D3AB4F

FASTA49655,800
        10         20         30         40         50         60 
MGRRALLLLL LSFLAPWATI ALRPALRALG SLHLPTNPTS LPAVAKNYSV LYFQQKVDHF 

        70         80         90        100        110        120 
GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC NNTGFMWDVA EELKAMLVFA 

       130        140        150        160        170        180 
EHRYYGESLP FGDNSFKDSR HLNFLTSEQA LADFAELIKH LKRTIPGAEN QPVIAIGGSY 

       190        200        210        220        230        240 
GGMLAAWFRM KYPHMVVGAL AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIHRS 

       250        260        270        280        290        300 
WDAINRLSNT GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP 

       310        320        330        340        350        360 
LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA TSSLGTLGWS 

       370        380        390        400        410        420 
YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV RPRPSWITTM YGGKNISSHT 

       430        440        450        460        470        480 
NIVFSNGELD PWSGGGVTKD ITDTLVAVTI SEGAHHLDLR TKNALDPMSV LLARSLEVRH 

       490 
MKNWIRDFYD SAGKQH 

« Hide

Isoform 2 [UniParc].

Checksum: A2490258A57E6F23
Show »

FASTA51758,100

References

« Hide 'large scale' references
[1]"Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families."
Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
J. Biol. Chem. 268:16631-16638(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Kidney.
[2]Erratum
Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
J. Biol. Chem. 268:26032-26032(1993)
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASP-112.
Tissue: Kidney and Lung.
[4]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[8]"Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney."
Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., Erdos E.G.
J. Biol. Chem. 253:5927-5931(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Kidney.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-415.
Tissue: Liver.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase."
Soisson S.M., Patel S.B., Abeywickrema P.D., Byrne N.J., Diehl R.E., Hall D.L., Ford R.E., Reid J.C., Rickert K.W., Shipman J.M., Sharma S., Lumb K.J.
BMC Struct. Biol. 10:16-16(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 46-491, SUBUNIT, DISULFIDE BONDS, ACTIVE SITE, GLYCOSYLATION AT ASN-101; ASN-317; ASN-336; ASN-345 AND ASN-415.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13977 mRNA. Translation: AAA99891.1.
AK091786 mRNA. Translation: BAG52417.1.
AK312919 mRNA. Translation: BAG35764.1.
AB451270 mRNA. Translation: BAG70084.1.
AB451397 mRNA. Translation: BAG70211.1.
AP000893 Genomic DNA. No translation available.
AP001646 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75074.1.
CH471076 Genomic DNA. Translation: EAW75075.1.
BC001500 mRNA. Translation: AAH01500.1.
CCDSCCDS41695.1. [P42785-2]
CCDS8262.1. [P42785-1]
PIRA47352.
RefSeqNP_005031.1. NM_005040.2. [P42785-1]
NP_955450.2. NM_199418.2. [P42785-2]
UniGeneHs.523936.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2ZX-ray2.79B46-491[»]
ProteinModelPortalP42785.
SMRP42785. Positions 46-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111538. 12 interactions.
IntActP42785. 4 interactions.
MINTMINT-3015634.
STRING9606.ENSP00000377055.

Chemistry

BindingDBP42785.
ChEMBLCHEMBL2335.

Protein family/group databases

MEROPSS28.001.

PTM databases

PhosphoSiteP42785.

Polymorphism databases

DMDM1172047.

Proteomic databases

MaxQBP42785.
PaxDbP42785.
PRIDEP42785.

Protocols and materials databases

DNASU5547.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313010; ENSP00000317362; ENSG00000137509. [P42785-1]
ENST00000393399; ENSP00000377055; ENSG00000137509. [P42785-2]
GeneID5547.
KEGGhsa:5547.
UCSCuc001ozs.3. human. [P42785-1]

Organism-specific databases

CTD5547.
GeneCardsGC11M082535.
HGNCHGNC:9344. PRCP.
HPAHPA017065.
MIM176785. gene.
neXtProtNX_P42785.
PharmGKBPA33705.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290141.
HOGENOMHOG000238311.
HOVERGENHBG005526.
KOK01285.
OMARSWKAIN.
OrthoDBEOG78WKRN.
PhylomeDBP42785.
TreeFamTF314414.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP42785.
BgeeP42785.
CleanExHS_PRCP.
GenevestigatorP42785.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERPTHR11010. PTHR11010. 1 hit.
PfamPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPRCP. human.
EvolutionaryTraceP42785.
GeneWikiPRCP.
GenomeRNAi5547.
NextBio21494.
PROP42785.
SOURCESearch...

Entry information

Entry namePCP_HUMAN
AccessionPrimary (citable) accession number: P42785
Secondary accession number(s): A8MU24 expand/collapse secondary AC list , B2R7B7, B3KRK5, B5BU34
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM