CPXM1_HUMAN
ID CPXM1_HUMAN Reviewed; 734 AA.
AC Q96SM3; Q6P4G8; Q6UW65; Q9NUB5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Probable carboxypeptidase X1;
DE EC=3.4.17.-;
DE AltName: Full=Metallocarboxypeptidase CPX-1;
DE Flags: Precursor;
GN Name=CPXM1; Synonyms=CPX1, CPXM; ORFNames=UNQ3015/PRO9782;
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 [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
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. No
CC carboxypeptidase activity was found yet (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; AK027661; BAB55275.1; -; mRNA.
DR EMBL; AY358956; AAQ89315.1; -; mRNA.
DR EMBL; AL035460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC063430; AAH63430.1; -; mRNA.
DR CCDS; CCDS13033.1; -.
DR RefSeq; NP_001171628.1; NM_001184699.1.
DR RefSeq; NP_062555.1; NM_019609.4.
DR AlphaFoldDB; Q96SM3; -.
DR SMR; Q96SM3; -.
DR BioGRID; 121127; 1.
DR IntAct; Q96SM3; 1.
DR STRING; 9606.ENSP00000369979; -.
DR MEROPS; M14.039; -.
DR GlyConnect; 1626; 2 N-Linked glycans (1 site).
DR GlyGen; Q96SM3; 8 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (2 sites).
DR iPTMnet; Q96SM3; -.
DR PhosphoSitePlus; Q96SM3; -.
DR BioMuta; CPXM1; -.
DR DMDM; 62512151; -.
DR EPD; Q96SM3; -.
DR jPOST; Q96SM3; -.
DR MassIVE; Q96SM3; -.
DR PaxDb; Q96SM3; -.
DR PeptideAtlas; Q96SM3; -.
DR PRIDE; Q96SM3; -.
DR ProteomicsDB; 78128; -.
DR Antibodypedia; 23301; 95 antibodies from 21 providers.
DR DNASU; 56265; -.
DR Ensembl; ENST00000380605.3; ENSP00000369979.2; ENSG00000088882.8.
DR GeneID; 56265; -.
DR KEGG; hsa:56265; -.
DR MANE-Select; ENST00000380605.3; ENSP00000369979.2; NM_019609.5; NP_062555.1.
DR UCSC; uc002wgu.4; human.
DR CTD; 56265; -.
DR DisGeNET; 56265; -.
DR GeneCards; CPXM1; -.
DR HGNC; HGNC:15771; CPXM1.
DR HPA; ENSG00000088882; Tissue enhanced (gallbladder).
DR MIM; 609555; gene.
DR neXtProt; NX_Q96SM3; -.
DR OpenTargets; ENSG00000088882; -.
DR PharmGKB; PA162382779; -.
DR VEuPathDB; HostDB:ENSG00000088882; -.
DR eggNOG; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000156141; -.
DR HOGENOM; CLU_006722_4_0_1; -.
DR InParanoid; Q96SM3; -.
DR OMA; TDRRPCH; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q96SM3; -.
DR TreeFam; TF315592; -.
DR PathwayCommons; Q96SM3; -.
DR SignaLink; Q96SM3; -.
DR BioGRID-ORCS; 56265; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; CPXM1; human.
DR GeneWiki; CPXM1; -.
DR GenomeRNAi; 56265; -.
DR Pharos; Q96SM3; Tdark.
DR PRO; PR:Q96SM3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96SM3; protein.
DR Bgee; ENSG00000088882; Expressed in decidua and 120 other tissues.
DR Genevisible; Q96SM3; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..734
FT /note="Probable carboxypeptidase X1"
FT /id="PRO_0000004407"
FT DOMAIN 113..274
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 30..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT CONFLICT 40
FT /note="S -> L (in Ref. 4; AAH63430)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Q -> H (in Ref. 2; AAQ89315)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="R -> W (in Ref. 1; BAB55275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 81668 MW; B1205522889F6FE5 CRC64;
MWGLLLALAA FAPAVGPALG APRNSVLGLA QPGTTKVPGS TPALHSSPAQ PPAETANGTS
EQHVRIRVIK KKKVIMKKRK KLTLTRPTPL VTAGPLVTPT PAGTLDPAEK QETGCPPLGL
ESLRVSDSRL EASSSQSFGL GPHRGRLNIQ SGLEDGDLYD GAWCAEEQDA DPWFQVDAGH
PTRFSGVITQ GRNSVWRYDW VTSYKVQFSN DSRTWWGSRN HSSGMDAVFP ANSDPETPVL
NLLPEPQVAR FIRLLPQTWL QGGAPCLRAE ILACPVSDPN DLFLEAPASG SSDPLDFQHH
NYKAMRKLMK QVQEQCPNIT RIYSIGKSYQ GLKLYVMEMS DKPGEHELGE PEVRYVAGMH
GNEALGRELL LLLMQFLCHE FLRGNPRVTR LLSEMRIHLL PSMNPDGYEI AYHRGSELVG
WAEGRWNNQS IDLNHNFADL NTPLWEAQDD GKVPHIVPNH HLPLPTYYTL PNATVAPETR
AVIKWMKRIP FVLSANLHGG ELVVSYPFDM TRTPWAAREL TPTPDDAVFR WLSTVYAGSN
LAMQDTSRRP CHSQDFSVHG NIINGADWHT VPGSMNDFSY LHTNCFEVTV ELSCDKFPHE
NELPQEWENN KDALLTYLEQ VRMGIAGVVR DKDTELGIAD AVIAVDGINH DVTTAWGGDY
WRLLTPGDYM VTASAEGYHS VTRNCRVTFE EGPFPCNFVL TKTPKQRLRE LLAAGAKVPP
DLRRRLERLR GQKD
