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 Q9JJN5

Entry ID Method Resolution Chain Position Source
AF-Q9JJN5-F1 Predicted AlphaFoldDB

23 variants for Q9JJN5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389540779 11 L>P No EVA
rs3389540815 17 F>L No EVA
rs3389546040 20 P>T No EVA
rs3389546029 45 I>T No EVA
rs3389546098 114 I>V No EVA
rs226465568 132 D>A No EVA
rs3389508621 146 G>R No EVA
rs214852067 176 N>Y No EVA
rs3389535164 183 L>Q No EVA
rs3389550765 227 D>E No EVA
rs3409476441 234 F>* No EVA
rs3412989279 237 P>H No EVA
rs3409711577 240 T>P No EVA
rs3409269456 241 S>A No EVA
rs3408891415 243 S>C No EVA
rs3389550801 276 P>L No EVA
rs3389546045 348 D>E No EVA
rs3389535197 384 T>P No EVA
rs3389550749 385 Y>C No EVA
rs3389543564 405 P>H No EVA
rs243025539 430 G>S No EVA
rs3389556625 438 K>M No EVA
rs3389536848 441 R>L No EVA

No associated diseases with Q9JJN5

1 regional properties for Q9JJN5

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 32 - 358 IPR017452

Functions

Description
EC Number 3.4.17.3 Metallocarboxypeptidases
Subcellular Localization
  • Secreted, extracellular space
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 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.

3 GO annotations of molecular function

Name Definition
carboxypeptidase activity Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain.
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.
zinc ion binding Binding to a zinc ion (Zn).

5 GO annotations of biological process

Name Definition
bradykinin catabolic process The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin.
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 catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
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.
response to glucocorticoid Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucocorticoid stimulus. Glucocorticoids are hormonal C21 corticosteroids synthesized from cholesterol with the ability to bind with the cortisol receptor and trigger similar effects. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects.

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
O75976 CPD Carboxypeptidase D 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
O89001 Cpd Carboxypeptidase D 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
A2RUV9 Aebp1 Adipocyte enhancer-binding protein 1 Rattus norvegicus (Rat) PR
Q9EQV8 Cpn1 Carboxypeptidase N catalytic chain Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MPDLPSAFLP LLLLSKFVTP VTFRHHRYDD LVRTLYKVHN QCPDITRLYN IGRSVKGRYL
70 80 90 100 110 120
YVLEFSDYPG IHEPLEPEVK YVGNMHGNEV LGRELLLQLS EFLCEEFRNR NQRILRLIQD
130 140 150 160 170 180
TRIHILPSMN PDGYEVAAAQ GPNMSGYLVG RNNANGVDLN RNFPDLNTYF YYNSKNGGPN
190 200 210 220 230 240
HHLPLPDNWK SQVEPETRAV IQWIRSLNFV LSANMHGGAV VANYPYDKSL EHRFRGPHRT
250 260 270 280 290 300
SNSPTPDDEL FQTLAKVYSY AHGWMHQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
310 320 330 340 350 360
NCFEITLELS CDKFPRQEEL QREWLGNREA LIQFLEQVHQ GIKGMVLDEN SNNLTGAVIS
370 380 390 400 410 420
VTGINHDVTS GEHGDYFRLL LPGTYSVTAK APGYDPKTVT VTVGPAGPTV VDFQLKRSSS
430 440 450
QVYPVQRAPG RGQGGRAKQP RTSRKKDPAT KRHRGPA