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 Q4ZJM7

Entry ID Method Resolution Chain Position Source
AF-Q4ZJM7-F1 Predicted AlphaFoldDB

20 variants for Q4ZJM7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs251273182 11 L>F No EVA
rs3388630228 19 V>M No EVA
rs238348388 20 A>G No EVA
rs3393177113 26 T>K No EVA
rs3388632217 30 K>R No EVA
rs3388632115 51 F>L No EVA
rs3388638066 83 G>A No EVA
rs3388635165 88 A>G No EVA
rs3388635176 89 T>I No EVA
rs248907808 91 R>H No EVA
rs260606842 140 S>I No EVA
rs3393196087 168 Q>K No EVA
rs3388624110 206 S>A No EVA
rs239358369 249 R>Q No EVA
rs3388635125 292 G>C No EVA
rs3388632271 345 V>I No EVA
rs3388632182 403 G>A No EVA
rs36663775 411 V>M No EVA
rs3413022446 464 D>H No EVA
rs37389056 479 S>R No EVA

No associated diseases with Q4ZJM7

3 regional properties for Q4ZJM7

Type Name Position InterPro Accession
domain C1q domain 341 - 478 IPR001073
repeat Collagen triple helix repeat 118 - 175 IPR008160-1
repeat Collagen triple helix repeat 244 - 341 IPR008160-2

Functions

Description
EC Number
Subcellular Localization
  • Secreted, extracellular space, extracellular matrix
  • Localized in both the surrounding otoconial matrix and otoconia
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
collagen type IV trimer A collagen heterotrimer containing type IV alpha chains; [alpha1(IV)]2alpha2(IV) trimers are commonly observed, although more type IV alpha chains exist and may be present in type IV trimers; type IV collagen triple helices associate to form 3 dimensional nets within basement membranes.
extracellular matrix A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
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
calcium ion binding Binding to a calcium ion (Ca2+).
extracellular matrix structural constituent The action of a molecule that contributes to the structural integrity of the extracellular matrix.

4 GO annotations of biological process

Name Definition
collagen-activated tyrosine kinase receptor signaling pathway The series of molecular signals initiated by collagen binding to its receptor on the surface of a target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription.
extracellular matrix organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
otolith mineralization The precipitation of specific crystal forms of calcium carbonate with extracellular matrix proteins in the otolith organs of the vertebrate inner ear.
protein homooligomerization The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MWIFSSLCAV LTILAMDDVA TEAKTTPYTK FTKKSEGKEM LKGLKPSSGF FLDGEETVHT
70 80 90 100 110 120
ETAAMAEPTT GSPALAMAES TAGPSASATT RLLPFESFSL DTTGFVLNCC HCCSFVTGQK
130 140 150 160 170 180
GEPGKMGKQG PKGETGDTGS PGHPGTTGPQ GPKGQKGEKG LKGDRGDQGA GGIPGYPGKP
190 200 210 220 230 240
GEQGALGPKG DKGTIGPAGT KGQKGSKGEL CGNGTKGEKG DPGASGAHGF IGEPGAKGEK
250 260 270 280 290 300
GGVGEKGYRG DLGERGEKGQ KGEKGMEGEK GSRGDVGSEG KRGSDGLPGL RGDSGPKGEK
310 320 330 340 350 360
GEIGSPGFTG PAGPKGELGS KGVRGPTGKK GSRGVKGSKG EATQVPQSAF SALLSKPFPP
370 380 390 400 410 420
PNVPIKFDKI LSNDQGDYSP VTGKFNCSVP GTYIFSYHVT VRGRPARISL VARNRKQFKS
430 440 450 460 470 480
RETLYGQQVD QASLLLILKL SAGDQVWLEV SKDWNGLYVG PEDDSIFSGF LLYPEETFSK
SP