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 Q9Z100

Entry ID Method Resolution Chain Position Source
AF-Q9Z100-F1 Predicted AlphaFoldDB

45 variants for Q9Z100

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388593683 31 P>S No EVA
rs1135167357 46 T>I No EVA
rs3388595688 53 E>V No EVA
rs27260711 67 V>I No EVA
rs244892897 76 H>Q No EVA
rs3388587155 76 H>Y No EVA
rs3388589260 77 P>S No EVA
rs13460790 78 G>S No EVA
rs213317939 86 V>L No EVA
rs249674882 88 P>T No EVA
rs227819030 91 P>S No EVA
rs3392135005 110 L>S No EVA
rs3388584781 180 Q>H No EVA
rs3388592534 202 S>C No EVA
rs3388580197 206 W>* No EVA
rs27260715 216 I>M No EVA
rs3388593743 242 R>L No EVA
rs27260717 253 A>V No EVA
rs3388593091 270 D>E No EVA
rs27260718 282 N>D No EVA
rs3388594019 282 N>T No EVA
rs3388580199 292 K>R No EVA
rs3388595683 332 P>T No EVA
rs3388589727 395 D>H No EVA
rs3388584793 429 L>I No EVA
rs225616334 444 D>H No EVA
rs3388585146 448 N>D No EVA
rs3388592736 462 A>T No EVA
rs3392245015 464 V>E No EVA
rs3391937071 465 A>P No EVA
rs3388589729 477 R>C No EVA
rs3388594001 480 F>C No EVA
rs3388590568 507 R>L No EVA
rs3388595682 514 D>Y No EVA
rs3388585070 539 P>S No EVA
rs3388595674 540 C>Y No EVA
rs3388585430 574 C>S No EVA
rs3388593983 578 T>I No EVA
rs3388588430 587 P>H No EVA
rs3388588373 601 D>N No EVA
rs3388592572 612 M>L No EVA
rs3388593114 651 R>G No EVA
rs3388588416 654 T>A No EVA
rs4223498 691 K>M No EVA
rs3388587966 717 R>Q No EVA

No associated diseases with Q9Z100

1 regional properties for Q9Z100

Type Name Position InterPro Accession
domain GPCR, rhodopsin-like, 7TM 21 - 279 IPR017452

Functions

Description
EC Number
Subcellular Localization
  • Secreted
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.

2 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.
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
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
P14384 CPM Carboxypeptidase M Homo sapiens (Human) PR
Q96SM3 CPXM1 Probable carboxypeptidase X1 Homo sapiens (Human) PR
O89001 Cpd Carboxypeptidase D Mus musculus (Mouse) PR
Q9JJN5 Cpn1 Carboxypeptidase N catalytic chain 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
MWGLLLAVTA FAPSVGLGLG APSASVPGLA PGSTLAPHSS VAQPSTKANE TSERHVRLRV
70 80 90 100 110 120
IKKKKIVVKK RKKLRHPGPL GTARPVVPTH PAKTLTLPEK QEPGCPPLGL ESLRVSDSQL
130 140 150 160 170 180
EASSSQSFGL GAHRGRLNIQ SGLEDGDLYD GAWCAEQQDT EPWLQVDAKN PVRFAGIVTQ
190 200 210 220 230 240
GRNSVWRYDW VTSFKVQFSN DSQTWWKSRN STGMDIVFPA NSDAETPVLN LLPEPQVARF
250 260 270 280 290 300
IRLLPQTWFQ GGAPCLRAEI LACPVSDPND LFPEAHTLGS SNSLDFRHHN YKAMRKLMKQ
310 320 330 340 350 360
VNEQCPNITR IYSIGKSHQG LKLYVMEMSD HPGEHELGEP EVRYVAGMHG NEALGRELLL
370 380 390 400 410 420
LLMQFLCHEF LRGDPRVTRL LTETRIHLLP SMNPDGYETA YHRGSELVGW AEGRWTHQGI
430 440 450 460 470 480
DLNHNFADLN TQLWYAEDDG LVPDTVPNHH LPLPTYYTLP NATVAPETWA VIKWMKRIPF
490 500 510 520 530 540
VLSANLHGGE LVVSYPFDMT RTPWAARELT PTPDDAVFRW LSTVYAGTNR AMQDTDRRPC
550 560 570 580 590 600
HSQDFSLHGN VINGADWHTV PGSMNDFSYL HTNCFEVTVE LSCDKFPHEK ELPQEWENNK
610 620 630 640 650 660
DALLTYLEQV RMGITGVVRD KDTELGIADA VIAVEGINHD VTTAWGGDYW RLLTPGDYVV
670 680 690 700 710 720
TASAEGYHTV RQHCQVTFEE GPVPCNFLLT KTPKERLREL LATRGKLPPD LRRKLERLRG
QK