CPN2_HUMAN
ID CPN2_HUMAN Reviewed; 545 AA.
AC P22792; B2RPE7; Q86SU4; Q8N5V4;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Carboxypeptidase N subunit 2;
DE AltName: Full=Carboxypeptidase N 83 kDa chain;
DE AltName: Full=Carboxypeptidase N large subunit;
DE AltName: Full=Carboxypeptidase N polypeptide 2;
DE AltName: Full=Carboxypeptidase N regulatory subunit;
DE Flags: Precursor;
GN Name=CPN2; Synonyms=ACBP;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-509 AND MET-536.
RC TISSUE=Hepatoblastoma;
RX PubMed=2378615; DOI=10.1016/s0021-9258(19)40187-7;
RA Tan F., Weerasinghe D.K., Skidgel R.A., Tamei H., Kaul R.K., Roninson I.B.,
RA Schilling J.W., Erdoes E.G.;
RT "The deduced protein sequence of the human carboxypeptidase N high
RT molecular weight subunit reveals the presence of leucine-rich tandem
RT repeats.";
RL J. Biol. Chem. 265:13-19(1990).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS; 82; 305; 379-426; 436; 445; 446 AND
RP 527-545.
RA Skidgel R.A.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3408501; DOI=10.1016/0006-291x(88)90284-7;
RA Skidgel R.A., Bennett C.D., Schilling J.W., Tan F., Weerasinghe D.K.,
RA Erdoes E.G.;
RT "Amino acid sequence of the N-terminus and selected tryptic peptides of the
RT active subunit of human plasma carboxypeptidase N: comparison with other
RT carboxypeptidases.";
RL Biochem. Biophys. Res. Commun. 154:1323-1329(1988).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348 AND ASN-359.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228 AND ASN-518.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
CC -!- FUNCTION: The 83 kDa subunit binds and stabilizes the catalytic subunit
CC at 37 degrees Celsius and keeps it in circulation. Under some
CC circumstances it may be an allosteric modifier of the catalytic
CC subunit.
CC -!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive
CC chains.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Whether or not any Cys residues participate in intrachain bonds is
CC unknown, but they do not form interchain disulfide bonds with the 50
CC kDa catalytic subunit.
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DR EMBL; J05158; AAA51921.2; -; mRNA.
DR EMBL; AC125362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC174158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031569; AAH31569.2; -; mRNA.
DR EMBL; BC042334; AAH42334.2; -; mRNA.
DR EMBL; BC137398; AAI37399.1; -; mRNA.
DR EMBL; BC137403; AAI37404.1; -; mRNA.
DR CCDS; CCDS33920.1; -.
DR PIR; A34901; A34901.
DR RefSeq; NP_001073982.3; NM_001080513.3.
DR RefSeq; NP_001278917.1; NM_001291988.1.
DR RefSeq; XP_005269337.1; XM_005269280.4.
DR AlphaFoldDB; P22792; -.
DR SMR; P22792; -.
DR BioGRID; 107762; 4.
DR CORUM; P22792; -.
DR IntAct; P22792; 2.
DR STRING; 9606.ENSP00000319464; -.
DR DrugBank; DB12271; ORE-1001.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MEROPS; M14.004; -.
DR MEROPS; X28.001; -.
DR GlyConnect; 1068; 7 N-Linked glycans (3 sites).
DR GlyGen; P22792; 8 sites, 10 N-linked glycans (3 sites).
DR iPTMnet; P22792; -.
DR PhosphoSitePlus; P22792; -.
DR BioMuta; CPN2; -.
DR DMDM; 334302917; -.
DR jPOST; P22792; -.
DR MassIVE; P22792; -.
DR PaxDb; P22792; -.
DR PeptideAtlas; P22792; -.
DR PRIDE; P22792; -.
DR ProteomicsDB; 54038; -.
DR Antibodypedia; 856; 198 antibodies from 29 providers.
DR DNASU; 1370; -.
DR Ensembl; ENST00000323830.4; ENSP00000319464.3; ENSG00000178772.7.
DR Ensembl; ENST00000429275.1; ENSP00000402232.1; ENSG00000178772.7.
DR GeneID; 1370; -.
DR KEGG; hsa:1370; -.
DR MANE-Select; ENST00000323830.4; ENSP00000319464.3; NM_001080513.4; NP_001073982.3.
DR UCSC; uc003fts.3; human.
DR CTD; 1370; -.
DR DisGeNET; 1370; -.
DR GeneCards; CPN2; -.
DR HGNC; HGNC:2313; CPN2.
DR HPA; ENSG00000178772; Tissue enriched (liver).
DR MIM; 603104; gene.
DR neXtProt; NX_P22792; -.
DR OpenTargets; ENSG00000178772; -.
DR PharmGKB; PA26830; -.
DR VEuPathDB; HostDB:ENSG00000178772; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000163072; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; P22792; -.
DR OMA; REVFCSD; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P22792; -.
DR TreeFam; TF351124; -.
DR PathwayCommons; P22792; -.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P22792; -.
DR BioGRID-ORCS; 1370; 11 hits in 1067 CRISPR screens.
DR GeneWiki; CPN2; -.
DR GenomeRNAi; 1370; -.
DR Pharos; P22792; Tdark.
DR PRO; PR:P22792; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P22792; protein.
DR Bgee; ENSG00000178772; Expressed in right lobe of liver and 47 other tissues.
DR Genevisible; P22792; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; NAS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; NAS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 11.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..545
FT /note="Carboxypeptidase N subunit 2"
FT /id="PRO_0000020989"
FT DOMAIN 22..49
FT /note="LRRNT"
FT REPEAT 98..119
FT /note="LRR 1"
FT REPEAT 122..143
FT /note="LRR 2"
FT REPEAT 146..167
FT /note="LRR 3"
FT REPEAT 170..191
FT /note="LRR 4"
FT REPEAT 194..215
FT /note="LRR 5"
FT REPEAT 218..239
FT /note="LRR 6"
FT REPEAT 242..263
FT /note="LRR 7"
FT REPEAT 266..287
FT /note="LRR 8"
FT REPEAT 290..311
FT /note="LRR 9"
FT REPEAT 314..335
FT /note="LRR 10"
FT REPEAT 338..359
FT /note="LRR 11"
FT REPEAT 362..383
FT /note="LRR 12"
FT DOMAIN 395..447
FT /note="LRRCT"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VARIANT 305
FT /note="A -> T (in dbSNP:rs3732477)"
FT /id="VAR_019722"
FT VARIANT 509
FT /note="Q -> R (in dbSNP:rs4974538)"
FT /evidence="ECO:0000269|PubMed:2378615"
FT /id="VAR_065186"
FT VARIANT 536
FT /note="V -> M (in dbSNP:rs11711157)"
FT /evidence="ECO:0000269|PubMed:2378615"
FT /id="VAR_019721"
FT CONFLICT 156
FT /note="Q -> R (in Ref. 4; AAH42334)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="Q -> W (in Ref. 4; AAH31569/AAH42334/AAI37399/
FT AAI37404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 60557 MW; 221AAF04413665AF CRC64;
MLPGAWLLWT SLLLLARPAQ PCPMGCDCFV QEVFCSDEEL ATVPLDIPPY TKNIIFVETS
FTTLETRAFG SNPNLTKVVF LNTQLCQFRP DAFGGLPRLE DLEVTGSSFL NLSTNIFSNL
TSLGKLTLNF NMLEALPEGL FQHLAALESL HLQGNQLQAL PRRLFQPLTH LKTLNLAQNL
LAQLPEELFH PLTSLQTLKL SNNALSGLPQ GVFGKLGSLQ ELFLDSNNIS ELPPQVFSQL
FCLERLWLQR NAITHLPLSI FASLGNLTFL SLQWNMLRVL PAGLFAHTPC LVGLSLTHNQ
LETVAEGTFA HLSNLRSLML SYNAITHLPA GIFRDLEELV KLYLGSNNLT ALHPALFQNL
SKLELLSLSK NQLTTLPEGI FDTNYNLFNL ALHGNPWQCD CHLAYLFNWL QQYTDRLLNI
QTYCAGPAYL KGQVVPALNE KQLVCPVTRD HLGFQVTWPD ESKAGGSWDL AVQERAARSQ
CTYSNPEGTV VLACDQAQCR WLNVQLSPQQ GSLGLQYNAS QEWDLRSSCG SLRLTVSIEA
RAAGP
