CPN2_MOUSE
ID CPN2_MOUSE Reviewed; 547 AA.
AC Q9DBB9; B2RR89; Q8R113;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
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;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Liver;
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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-111; ASN-119; ASN-348;
RP ASN-359 AND ASN-367.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: 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 subunit
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive
CC chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25836.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005049; BAB23775.1; ALT_INIT; mRNA.
DR EMBL; BC025836; AAH25836.1; ALT_INIT; mRNA.
DR EMBL; BC138287; AAI38288.1; -; mRNA.
DR EMBL; BC138288; AAI38289.1; -; mRNA.
DR CCDS; CCDS49819.1; -.
DR RefSeq; NP_082180.2; NM_027904.3.
DR RefSeq; XP_006522648.1; XM_006522585.1.
DR AlphaFoldDB; Q9DBB9; -.
DR SMR; Q9DBB9; -.
DR BioGRID; 214904; 3.
DR STRING; 10090.ENSMUSP00000069318; -.
DR GlyGen; Q9DBB9; 9 sites.
DR iPTMnet; Q9DBB9; -.
DR PhosphoSitePlus; Q9DBB9; -.
DR CPTAC; non-CPTAC-3428; -.
DR CPTAC; non-CPTAC-5598; -.
DR MaxQB; Q9DBB9; -.
DR PaxDb; Q9DBB9; -.
DR PeptideAtlas; Q9DBB9; -.
DR PRIDE; Q9DBB9; -.
DR ProteomicsDB; 285291; -.
DR Antibodypedia; 856; 198 antibodies from 29 providers.
DR DNASU; 71756; -.
DR Ensembl; ENSMUST00000064856; ENSMUSP00000069318; ENSMUSG00000023176.
DR GeneID; 71756; -.
DR KEGG; mmu:71756; -.
DR UCSC; uc007ywm.1; mouse.
DR CTD; 1370; -.
DR MGI; MGI:1919006; Cpn2.
DR VEuPathDB; HostDB:ENSMUSG00000023176; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000163072; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; Q9DBB9; -.
DR OMA; REVFCSD; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9DBB9; -.
DR TreeFam; TF351124; -.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 71756; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9DBB9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9DBB9; protein.
DR Bgee; ENSMUSG00000023176; Expressed in left lobe of liver and 26 other tissues.
DR Genevisible; Q9DBB9; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
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 Glycoprotein; Leucine-rich repeat; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..547
FT /note="Carboxypeptidase N subunit 2"
FT /id="PRO_0000020990"
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:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 547 AA; 60479 MW; 89437E8F32DA1453 CRC64;
MFPGAWLCWV SLLLLARLTQ PCPVGCDCFG REVFCSDEQL ADIPPDIPPH ITDIVFVETA
FTTVRTRAFS GSPNLTKVVF LNTQVRHLEP DAFGGLPRLQ DLEITGSPVS NLSAHIFSNL
SSLEKLTLDF DRLAGLPEDL FCHMDILESL QLQGNQLRTL PGRLFQSLRD LRTLNLAQNL
LTQLPKGAFQ SLTGLQMLKL SNNMLARLPE GALGSLSSLQ ELFLDGNAIT ELSPHLFSQL
FSLEMLWLQH NAICHLPVSL FSSLHNLTFL SLKDNALRTL PEGLFAHNQG LLHLSLSYNQ
LETIPEGAFT NLSRLVSLTL SHNAITDLPE HVFRNLEQLV KLSLDSNNLT ALHPALFHNL
SRLQLLNLSR NQLTTLPGGI FDTNYDLFNL ALLGNPWQCD CHLSYLTSWL RLYNNQISNT
HTFCAGPAYL KGQLVPNLKQ EQLICPVNPG HLSFRALGLD EGEPAGSWDL TVEGRAAHSQ
CAYSNPEGTV LLACEESRCR WLNIQLSSRD GSDSAAMVYN SSQEWGLRSS CGLLRVTVSI
EAPAAGP
