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 Q29GR8

Entry ID Method Resolution Chain Position Source
AF-Q29GR8-F1 Predicted AlphaFoldDB

No variants for Q29GR8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q29GR8

No associated diseases with Q29GR8

10 regional properties for Q29GR8

Type Name Position InterPro Accession
domain FERM domain 24 - 314 IPR000299
domain Ezrin/radixin/moesin, C-terminal 519 - 593 IPR011259
domain FERM, N-terminal 28 - 89 IPR018979
domain FERM, C-terminal PH-like domain 229 - 318 IPR018980
conserved_site FERM conserved site 77 - 107 IPR019747-1
conserved_site FERM conserved site 195 - 224 IPR019747-2
domain FERM central domain 111 - 225 IPR019748
domain Band 4.1 domain 20 - 225 IPR019749
domain ERM family, FERM domain C-lobe 219 - 315 IPR041789
domain Ezrin/radixin/moesin, alpha-helical domain 349 - 468 IPR046810

Functions

Description
EC Number
Subcellular Localization
  • Cell junction, adherens junction
  • Cell projection, microvillus
  • Cell projection, rhabdomere
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cytoplasm, cytoskeleton
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
adherens junction A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

1 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.

3 GO annotations of biological process

Name Definition
animal organ morphogenesis Morphogenesis of an animal organ. An organ is defined as a tissue or set of tissues that work together to perform a specific function or functions. Morphogenesis is the process in which anatomical structures are generated and organized. Organs are commonly observed as visibly distinct structures, but may also exist as loosely associated clusters of cells that work together to perform a specific function or functions.
establishment or maintenance of epithelial cell apical/basal polarity Any cellular process that results in the specification, formation or maintenance of the apicobasal polarity of an epithelial cell.
neuron differentiation The process in which a relatively unspecialized cell acquires specialized features of a neuron.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVVVSDSRVR MPRYGGVSVK RKTLNVRVTT MDAELEFAIQ STTTGKQLFD QVVKTIGLRE
70 80 90 100 110 120
VWFFGLQYTD SKGDSTWIKL YKKVMNQDVK KENPLQFRFR AKFYPEDVAE ELIQDITLRL
130 140 150 160 170 180
FYLQVKNAIL TDEIYCPPET SVLLASYAVQ ARHGDHNKTT HTAGFLANDR LLPQRVIDQH
190 200 210 220 230 240
KMSKDEWEQS IMTWWQEHRS MLREDAMMEY LKIAQDLEMY GVNYFEIRNK KGTDLWLGVD
250 260 270 280 290 300
ALGLNIYEQD DRLTPKIGFP WSEIRNISFS EKKFIIKPID KKAPDFMFFA PRVRINKRIL
310 320 330 340 350 360
ALCMGNHELY MRRRKPDTID VQQMKAQARE EKNAKQQERE KLQLALAARE RAEKKQQEYE
370 380 390 400 410 420
DRLKQMQEEM ERSQRDLLEA QEMIRRLEEQ LKQLQAAKDE LELRQKELQS MLQRLEEAKN
430 440 450 460 470 480
MEAVEKIKLE EEIMAKQMEV QRIQDEVNAK DEETKRLQDE VEEARRKQAE AAAALLAAST
490 500 510 520 530 540
TPQHHHVAED ENENEEELTN GDAGGDVSRD LDTDEHIKDP IEDRRTLAER NERLHDQLKA
550 560 570 580 590
LKQDLAQSRD ETKETANDKI HRENVRQGRD KYKTLREIRK GNTKRRVDQF ENM