CPXM2_MOUSE
ID CPXM2_MOUSE Reviewed; 764 AA.
AC Q9D2L5; O54860; Q8VDQ4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Inactive carboxypeptidase-like protein X2;
DE Flags: Precursor;
GN Name=Cpxm2; Synonyms=Cpx2;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart, and Kidney;
RX PubMed=9809751; DOI=10.1089/dna.1998.17.897;
RA Xin X., Day R., Dong W., Lei Y., Fricker L.D.;
RT "Identification of mouse CPX-2, a novel member of the
RT metallocarboxypeptidase gene family: cDNA cloning, mRNA distribution, and
RT protein expression and characterization.";
RL DNA Cell Biol. 17:897-909(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: May be involved in cell-cell interactions.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung and kidney. Moderate
CC expression in liver and brain, including the cerebral cortex, piriform
CC cortex, nucleus of the lateral olfactory tract, hippocampus, habenular
CC nucleus, and choroid plexus. {ECO:0000269|PubMed:9809751}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Although related to peptidase M14 family, lacks the active
CC site residues and zinc-binding sites, suggesting that it has no
CC carboxypeptidase activity. {ECO:0000305}.
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DR EMBL; AF017639; AAC04670.1; -; mRNA.
DR EMBL; AK019509; BAB31768.1; -; mRNA.
DR EMBL; BC021444; AAH21444.1; -; mRNA.
DR CCDS; CCDS21921.1; -.
DR RefSeq; NP_061355.3; NM_018867.5.
DR AlphaFoldDB; Q9D2L5; -.
DR SMR; Q9D2L5; -.
DR STRING; 10090.ENSMUSP00000033149; -.
DR MEROPS; M14.953; -.
DR GlyGen; Q9D2L5; 5 sites.
DR iPTMnet; Q9D2L5; -.
DR PhosphoSitePlus; Q9D2L5; -.
DR MaxQB; Q9D2L5; -.
DR PaxDb; Q9D2L5; -.
DR PeptideAtlas; Q9D2L5; -.
DR PRIDE; Q9D2L5; -.
DR ProteomicsDB; 284158; -.
DR DNASU; 55987; -.
DR GeneID; 55987; -.
DR KEGG; mmu:55987; -.
DR UCSC; uc009kbu.2; mouse.
DR CTD; 119587; -.
DR MGI; MGI:1926006; Cpxm2.
DR eggNOG; KOG2649; Eukaryota.
DR InParanoid; Q9D2L5; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q9D2L5; -.
DR TreeFam; TF315592; -.
DR BioGRID-ORCS; 55987; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cpxm2; mouse.
DR PRO; PR:Q9D2L5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D2L5; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd00057; FA58C; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..764
FT /note="Inactive carboxypeptidase-like protein X2"
FT /id="PRO_0000004410"
FT DOMAIN 142..301
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 71..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT CONFLICT 49
FT /note="Y -> H (in Ref. 2; AAH21444)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Q -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="M -> L (in Ref. 2; AAH21444)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="H -> Q (in Ref. 2; AAH21444)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="S -> L (in Ref. 2; AAH21444)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="S -> T (in Ref. 2; AAH21444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 86963 MW; 2813CBBE0C5A149A CRC64;
MARLGTACPA LALALALVAV ALAGVRAQGA AFEEPDYYSQ ELWRRGRYYG HPEPEPEQEL
FSPSMHEDLR VEEQEQQEPH QQGHRTPKKA IKPKKAPKRE KLVAETPPPG KNSNRKGRRS
KNLEKAASDD HGVPVAHEDV RESCPPLGLE TLKITDFQLH ASTSKRYGLG AHRGRLNIQA
GINENDFYDG AWCAGRNDLH QWIEVDARRL TKFTGVITQG RNSLWLSDWV TSYKVMVSND
SHTWVTVKNG SGDMIFEGNS EKEIPVLNEL PVPMVARYIR INPQSWFDNG SICMRMEILG
CPLPDPNNYY HRRNEMTTTD DLDFKHHNYK EMRQLMKVVN EMCPNITRIY NIGKSHQGLK
LYAVEISDHP GEHEVGEPEF HYIAGAHGNE VLGRELLLLL LHFLCQEYSA QNARIVRLVE
ETRIHILPSL NPDGYEKAYE GGSELGGWSL GRWTHDGIDI NNNFPDLNSL LWEAEDQQNA
PRKVPNHYIA IPEWFLSENA TVATETRAVI AWMEKIPFVL GGNLQGGELV VAYPYDMVRS
LWKTQEHTPT PDDHVFRWLA YSYASTHRLM TDARRRVCHT EDFQKEEGTV NGASWHTVAG
SLNDFSYLHT NCFELSIYVG CDKYPHESEL PEEWENNRES LIVFMEQVHR GIKGIVRDLQ
GKGISNAVIS VEGVNHDIRT ASDGDYWRLL NPGEYVVTAK AEGFITSTKN CMVGYDMGAT
RCDFTLTKTN LARIREIMET FGKQPVSLPS RRLKLRGRKR RQRG
