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Protein

Inactive carboxypeptidase-like protein X2

Gene

Cpxm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

May be involved in cell-cell interactions.

GO - Molecular functioni

Complete GO annotation...

Protein family/group databases

MEROPSiM14.953.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive carboxypeptidase-like protein X2
Gene namesi
Name:Cpxm2
Synonyms:Cpx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1926006. Cpxm2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 764737Inactive carboxypeptidase-like protein X2PRO_0000004410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi144 ↔ 301PROSITE-ProRule annotation
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9D2L5.
PaxDbiQ9D2L5.
PRIDEiQ9D2L5.

PTM databases

iPTMnetiQ9D2L5.
PhosphoSiteiQ9D2L5.

Expressioni

Tissue specificityi

Highly expressed in lung and kidney. Moderate expression in liver and brain, including the cerebral cortex, piriform cortex, nucleus of the lateral olfactory tract, hippocampus, habenular nucleus, and choroid plexus.1 Publication

Gene expression databases

BgeeiQ9D2L5.
CleanExiMM_CPXM2.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033149.

Structurei

3D structure databases

ProteinModelPortaliQ9D2L5.
SMRiQ9D2L5. Positions 143-301, 322-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini142 – 301160F5/8 type CPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi396 – 4016Poly-Leu

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated
Contains 1 F5/8 type C domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiQ9D2L5.
KOiK08639.
OrthoDBiEOG7B8S32.
PhylomeDBiQ9D2L5.
TreeFamiTF315592.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00231. FA58C. 1 hit.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D2L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLGTACPA LALALALVAV ALAGVRAQGA AFEEPDYYSQ ELWRRGRYYG
60 70 80 90 100
HPEPEPEQEL FSPSMHEDLR VEEQEQQEPH QQGHRTPKKA IKPKKAPKRE
110 120 130 140 150
KLVAETPPPG KNSNRKGRRS KNLEKAASDD HGVPVAHEDV RESCPPLGLE
160 170 180 190 200
TLKITDFQLH ASTSKRYGLG AHRGRLNIQA GINENDFYDG AWCAGRNDLH
210 220 230 240 250
QWIEVDARRL TKFTGVITQG RNSLWLSDWV TSYKVMVSND SHTWVTVKNG
260 270 280 290 300
SGDMIFEGNS EKEIPVLNEL PVPMVARYIR INPQSWFDNG SICMRMEILG
310 320 330 340 350
CPLPDPNNYY HRRNEMTTTD DLDFKHHNYK EMRQLMKVVN EMCPNITRIY
360 370 380 390 400
NIGKSHQGLK LYAVEISDHP GEHEVGEPEF HYIAGAHGNE VLGRELLLLL
410 420 430 440 450
LHFLCQEYSA QNARIVRLVE ETRIHILPSL NPDGYEKAYE GGSELGGWSL
460 470 480 490 500
GRWTHDGIDI NNNFPDLNSL LWEAEDQQNA PRKVPNHYIA IPEWFLSENA
510 520 530 540 550
TVATETRAVI AWMEKIPFVL GGNLQGGELV VAYPYDMVRS LWKTQEHTPT
560 570 580 590 600
PDDHVFRWLA YSYASTHRLM TDARRRVCHT EDFQKEEGTV NGASWHTVAG
610 620 630 640 650
SLNDFSYLHT NCFELSIYVG CDKYPHESEL PEEWENNRES LIVFMEQVHR
660 670 680 690 700
GIKGIVRDLQ GKGISNAVIS VEGVNHDIRT ASDGDYWRLL NPGEYVVTAK
710 720 730 740 750
AEGFITSTKN CMVGYDMGAT RCDFTLTKTN LARIREIMET FGKQPVSLPS
760
RRLKLRGRKR RQRG
Length:764
Mass (Da):86,963
Last modified:June 1, 2001 - v1
Checksum:i2813CBBE0C5A149A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491Y → H in AAH21444 (PubMed:16141072).Curated
Sequence conflicti58 – 581Q → P (PubMed:9809751).Curated
Sequence conflicti58 – 581Q → P (PubMed:16141072).Curated
Sequence conflicti65 – 651M → L in AAH21444 (PubMed:16141072).Curated
Sequence conflicti402 – 4021H → Q in AAH21444 (PubMed:16141072).Curated
Sequence conflicti409 – 4091S → L in AAH21444 (PubMed:16141072).Curated
Sequence conflicti469 – 4691S → T in AAH21444 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017639 mRNA. Translation: AAC04670.1.
AK019509 mRNA. Translation: BAB31768.1.
BC021444 mRNA. Translation: AAH21444.1.
CCDSiCCDS21921.1.
RefSeqiNP_061355.3. NM_018867.5.
UniGeneiMm.471654.

Genome annotation databases

GeneIDi55987.
KEGGimmu:55987.
UCSCiuc009kbu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017639 mRNA. Translation: AAC04670.1.
AK019509 mRNA. Translation: BAB31768.1.
BC021444 mRNA. Translation: AAH21444.1.
CCDSiCCDS21921.1.
RefSeqiNP_061355.3. NM_018867.5.
UniGeneiMm.471654.

3D structure databases

ProteinModelPortaliQ9D2L5.
SMRiQ9D2L5. Positions 143-301, 322-714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033149.

Protein family/group databases

MEROPSiM14.953.

PTM databases

iPTMnetiQ9D2L5.
PhosphoSiteiQ9D2L5.

Proteomic databases

MaxQBiQ9D2L5.
PaxDbiQ9D2L5.
PRIDEiQ9D2L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi55987.
KEGGimmu:55987.
UCSCiuc009kbu.2. mouse.

Organism-specific databases

CTDi119587.
MGIiMGI:1926006. Cpxm2.

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiQ9D2L5.
KOiK08639.
OrthoDBiEOG7B8S32.
PhylomeDBiQ9D2L5.
TreeFamiTF315592.

Miscellaneous databases

ChiTaRSiCpxm2. mouse.
PROiQ9D2L5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D2L5.
CleanExiMM_CPXM2.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR000834. Peptidase_M14.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
PF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00231. FA58C. 1 hit.
SM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of mouse CPX-2, a novel member of the metallocarboxypeptidase gene family: cDNA cloning, mRNA distribution, and protein expression and characterization."
    Xin X., Day R., Dong W., Lei Y., Fricker L.D.
    DNA Cell Biol. 17:897-909(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Heart and Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  3. "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].
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCPXM2_MOUSE
AccessioniPrimary (citable) accession number: Q9D2L5
Secondary accession number(s): O54860, Q8VDQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although related to peptidase M14 family, lacks the active sites residues and zinc-binding sites, suggesting that it has no carboxypeptidase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.