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 Q8R4H4

Entry ID Method Resolution Chain Position Source
AF-Q8R4H4-F1 Predicted AlphaFoldDB

37 variants for Q8R4H4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs226219823 3 G>S No EVA
rs3388820911 9 L>V No EVA
rs3388824060 10 V>D No EVA
rs244798995 16 L>V No EVA
rs212602970 19 R>Q No EVA
rs3388813234 23 F>C No EVA
rs230993737 25 N>S No EVA
rs3388809867 47 A>T No EVA
rs16800316 100 G>S No EVA
rs249821913 105 I>V No EVA
rs3388819172 146 Y>F No EVA
rs3388816428 164 H>L No EVA
rs3388819231 183 G>D No EVA
rs3396350698 184 P>Q No EVA
rs3396616098 184 P>T No EVA
rs3396588310 190 W>NESQCQSR* No EVA
rs3396771871 209 I>V No EVA
rs240263155 215 N>D No EVA
rs257524779 228 N>S No EVA
rs3388787494 236 I>N No EVA
rs3388799172 245 F>L No EVA
rs3388799174 271 N>K No EVA
rs248012821 276 A>T No EVA
rs3388820933 282 G>D No EVA
rs3396350650 293 R>L* No EVA
rs3396662269 294 G>L No EVA
rs3388808263 315 N>I No EVA
rs264686286 344 E>D No EVA
rs36418096 358 N>Y No EVA
rs3396439119 379 G>E No EVA
rs3396667260 383 D>V No EVA
rs3396350673 387 D>E No EVA
rs3396599083 387 D>N No EVA
rs3388824073 413 I>N No EVA
rs3388808233 417 A>G No EVA
rs3388787474 420 T>I No EVA
rs3388809861 430 H>R No EVA

No associated diseases with Q8R4H4

3 regional properties for Q8R4H4

Type Name Position InterPro Accession
domain Peptidase M14, carboxypeptidase A 139 - 422 IPR000834
domain Carboxypeptidase, activation peptide 43 - 117 IPR003146
domain Carboxypeptidase A, carboxypeptidase domain 134 - 434 IPR034248

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.

3 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.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQGTQRGGLV PGLSPLDRRT LLFCNFILAV AWGQVNFTGD QVLRVLAKNE KQLSLLRDLE
70 80 90 100 110 120
TQKPQKVDFW RGPARPSLPV DMRVPFSELP SVKAYLKSHG LAYSIMIKDI QVLLDEERDA
130 140 150 160 170 180
MAKSRRLERS TNSFSYSSYH TLDEIYSWID NFVAEHSNLV SKIHIGKSFE NRSILVLKFS
190 200 210 220 230 240
TGGPNRPAIW IDTGIHSREW ITHATGIWIS QKIVNAYGKD HVLKRILNTM DIFIEIVTNP
250 260 270 280 290 300
DGFAFTHSMN RLWRKNKSSQ PGIFCIGVDL NRNWKAGFGG NGSNKNPCSE TYRGPAPESE
310 320 330 340 350 360
PEVAAIVDFI TGHGNFKAMI SIHSYSQMVM YPYGHSLEPV PNHEELFNLA KDAVKALNKV
370 380 390 400 410 420
HGIQYIFGSI STTLYSASGI SVDWAYDSGI KYAFSFELRD TGQYGFLLPA SQIVPTAEET
430
WMALQTIMKH TLNHPY