O89001
Gene name |
Cpd |
Protein name |
Carboxypeptidase D |
Names |
Metallocarboxypeptidase D, gp180 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:12874 |
EC number |
3.4.17.22: Metallocarboxypeptidases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O89001
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O89001-F1 | Predicted | AlphaFoldDB |
58 variants for O89001
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs261497502 | 6 | D>N | No | EVA | |
| rs237913787 | 35 | A>T | No | EVA | |
| rs3402462067 | 208 | D>V | No | EVA | |
| rs3389156038 | 250 | V>M | No | EVA | |
| rs3389191994 | 277 | L>F | No | EVA | |
| rs3389117973 | 303 | T>I | No | EVA | |
| rs3389175438 | 316 | F>L | No | EVA | |
| rs3389181498 | 319 | G>W | No | EVA | |
| rs3410333687 | 356 | P>Q | No | EVA | |
| rs3401859298 | 404 | A>V | No | EVA | |
| rs3389181565 | 428 | N>S | No | EVA | |
| rs3389192059 | 429 | L>I | No | EVA | |
| rs3389152109 | 442 | N>H | No | EVA | |
| rs16812428 | 445 | M>I | No | EVA | |
| rs3389182742 | 453 | E>V | No | EVA | |
| rs3401859250 | 509 | E>Q | No | EVA | |
| rs3389177836 | 599 | I>F | No | EVA | |
| rs3389156124 | 611 | E>G | No | EVA | |
| rs3389182816 | 617 | D>Y | No | EVA | |
| rs13459918 | 648 | Q>* | No | EVA | |
| rs3389169383 | 649 | P>S | No | EVA | |
| rs3389177869 | 666 | S>T | No | EVA | |
| rs3389175532 | 718 | P>S | No | EVA | |
| rs3389117932 | 738 | W>* | No | EVA | |
| rs3389144266 | 798 | F>L | No | EVA | |
| rs3389152131 | 801 | D>V | No | EVA | |
| rs3389117933 | 806 | R>K | No | EVA | |
| rs3389181532 | 815 | V>I | No | EVA | |
| rs3389169344 | 818 | I>T | No | EVA | |
| rs3389177801 | 835 | V>I | No | EVA | |
| rs3389177856 | 838 | T>S | No | EVA | |
| rs3402433053 | 858 | R>VKLT* | No | EVA | |
| rs3402228678 | 884 | R>S | No | EVA | |
| rs3402756316 | 885 | G>R | No | EVA | |
| rs3389189264 | 917 | F>S | No | EVA | |
| rs16812603 | 924 | D>N | No | EVA | |
| rs16812601 | 941 | R>K | No | EVA | |
| rs3389192017 | 1012 | Y>N | No | EVA | |
| rs1133606680 | 1016 | P>S | No | EVA | |
| rs3389193680 | 1027 | I>T | No | EVA | |
| rs3389185661 | 1083 | K>R | No | EVA | |
| rs3389144296 | 1112 | N>H | No | EVA | |
| rs3389189341 | 1117 | K>N | No | EVA | |
| rs3389152101 | 1133 | G>S | No | EVA | |
| rs3389117897 | 1149 | V>M | No | EVA | |
| rs3389175502 | 1171 | H>Q | No | EVA | |
| rs3389175447 | 1179 | T>A | No | EVA | |
| rs3389182774 | 1182 | C>* | No | EVA | |
| rs3389181484 | 1183 | Y>F | No | EVA | |
| rs3389191987 | 1186 | S>G | No | EVA | |
| rs3402457703 | 1196 | E>G | No | EVA | |
| rs228130177 | 1236 | K>I | No | EVA | |
| rs3402460962 | 1261 | D>A | No | EVA | |
| rs3401858386 | 1265 | Q>H | No | EVA | |
| rs3401858336 | 1265 | Q>LR* | No | EVA | |
| rs3401821906 | 1267 | H>Q | No | EVA | |
| rs3389152082 | 1289 | R>L | No | EVA | |
| rs3389192062 | 1291 | F>S | No | EVA |
No associated diseases with O89001
1 regional properties for O89001
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GPCR, rhodopsin-like, 7TM | 65 - 316 | IPR017452 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.17.22 | Metallocarboxypeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| trans-Golgi network | The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| metallocarboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| protein phosphatase 2A binding | Binding to protein phosphatase 2A. |
| protein-containing complex binding | Binding to a macromolecular complex. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| peptide metabolic process | The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. |
| protein processing | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
16 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P04836 | CPE | Carboxypeptidase E | Bos taurus (Bovine) | PR |
| Q2KJ83 | CPN1 | Carboxypeptidase N catalytic chain | Bos taurus (Bovine) | PR |
| Q8QGP3 | CPZ | Carboxypeptidase Z | Gallus gallus (Chicken) | PR |
| Q8IUX7 | AEBP1 | Adipocyte enhancer-binding protein 1 | Homo sapiens (Human) | PR |
| Q8N436 | CPXM2 | Inactive carboxypeptidase-like protein X2 | Homo sapiens (Human) | PR |
| Q66K79 | CPZ | Carboxypeptidase Z | Homo sapiens (Human) | PR |
| Q96SM3 | CPXM1 | Probable carboxypeptidase X1 | Homo sapiens (Human) | PR |
| P14384 | CPM | Carboxypeptidase M | Homo sapiens (Human) | PR |
| O75976 | CPD | Carboxypeptidase D | Homo sapiens (Human) | PR |
| Q9JJN5 | Cpn1 | Carboxypeptidase N catalytic chain | Mus musculus (Mouse) | PR |
| Q9Z100 | Cpxm1 | Probable carboxypeptidase X1 | Mus musculus (Mouse) | PR |
| Q80V42 | Cpm | Carboxypeptidase M | Mus musculus (Mouse) | PR |
| Q9D2L5 | Cpxm2 | Inactive carboxypeptidase-like protein X2 | Mus musculus (Mouse) | PR |
| Q640N1 | Aebp1 | Adipocyte enhancer-binding protein 1 | Mus musculus (Mouse) | PR |
| Q9EQV8 | Cpn1 | Carboxypeptidase N catalytic chain | Rattus norvegicus (Rat) | PR |
| A2RUV9 | Aebp1 | Adipocyte enhancer-binding protein 1 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASGRDERPP | WRLGRLRLLP | PPPLLLLLLL | LRSSAQAAHI | KKAEATTTTV | GGSEAAEGQF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DHYYHEAALG | EALEAAAAAG | PPGLARLFSI | GSSVEGRPLW | VLRLTAGLGP | PPTAAAGLDA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AGPLLPGRPQ | VKLVGNMHGD | ETVSRQVLVY | LARELASGYR | RGDPRLVRLL | NTTDVYLLPS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LNPDGFERAR | EGDCGLGDSG | PPGTSGRDNS | RGRDLNRSFP | DQFSTGEPPS | LDEVPEVRAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IDWIRRNKFV | LSGNLHGGSV | VASYPFDDSP | EHKTTGLYSK | TSDDEVFRYL | AKAYASNHPI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MKTGEPHCPG | DEDETFKDGI | TNGAHWYDVE | GGMQDYNYVW | ANCFEITLEL | SCCKYPPASQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LRQEWENNRE | SLITLIEKVH | IGIKGFVKDS | VTGSGLENAT | ISVAGINHNI | TTGRFGDFHR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LLVPGTYNLT | ALSTGYMPLT | INNIMVKEGP | ATEMDFSLRP | TVMSVMPGST | EAVTTPGTVA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VPNIPPGTPS | SHQPIQPKDF | HHHHFPDMEI | FLRRFANEYP | NITRLYSLGK | SVESRELYVM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EISDNPGVHE | PGEPEFKYIG | NMHGNEVVGR | ELLLNLIEYL | CKNFGTDPEV | TDLVRSTRIH |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LMPSMNPDGY | EKSQEGDSIS | VVGRNNSNNF | DLNRNFPDQF | VPITEPTQPE | TIAVMSWVKA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YPFVLSANLH | GGSLVVNYPY | DDNEQGVATY | SKSPDDAVFQ | QIALSYSKEN | SQMFQGRPCK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DMYLNEYFPH | GITNGASWYN | VPGGMQDWNY | LQTNCFEVTI | ELGCVKYPFE | NELPKYWEQN |
| 790 | 800 | 810 | 820 | 830 | 840 |
| RRSLIQFMKQ | VHQGVKGFVL | DATDGRGILN | ATLSVAEINH | PVTTYKAGDY | WRLLVPGTYK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ITASARGYNP | VTKNVTVRSE | GAVQVNFTLV | RSSADANNES | KKGRGHSTST | DDTSDPTSKE |
| 910 | 920 | 930 | 940 | 950 | 960 |
| FEALIKHLSA | ENGLEGFMLS | SSSDLALYRY | HSYKDLSEFL | RGLVMNYPHI | TNLTTLGQSV |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| EYRHIWSLEI | SNKPNISEPE | EPKIRFVAGI | HGNAPVGTEL | LLALAEFLCL | NYKRNPVVTQ |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LVDRTRIVIV | PSLNPDGRER | AQEKDCTSKT | GHTNAHGKDL | DTDFTSNASQ | PETKAIIENL |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| IQKQDFSLSI | ALDGGSVLVT | YPYDKPVQTV | ENKETLKHLA | SLYANNHPSM | HMGQPSCPNN |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| SDENIPGGVM | RGAEWHSHLG | SMKDYSVTYG | HCPEITVYTS | CCYFPSAAQL | PALWAENKKS |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| LLSMLVEVHK | GVHGLVKDKA | GKPISKAVIV | LNEGIKVYTK | EGGYFHVLLA | PGVHNINAIA |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| DGYQQQHTQV | FVHHDAASSV | VIVFDTDNRI | FGLPRELVVT | VSGATMSALI | LTACIIWCIC |
| 1330 | 1340 | 1350 | 1360 | 1370 | |
| SIKSNRHKDG | FHRLRQHHDE | YEDEIRMMST | GSKKSLLSHE | FQDETDTEEE | TLYSSKH |