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
  • Cell membrane ; Single-pass type I membrane protein
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