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 Q58CU2

Entry ID Method Resolution Chain Position Source
AF-Q58CU2-F1 Predicted AlphaFoldDB

66 variants for Q58CU2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs526558474 6 R>C No EVA
rs526840790 14 M>I No EVA
rs437667333 16 K>* No EVA
rs452072639 18 A>D No EVA
rs454538749 20 K>N No EVA
rs474645355 26 A>G No EVA
rs439967422 27 Q>L No EVA
rs438972573 33 I>M No EVA
rs473718847 33 I>N No EVA
rs458936939 34 P>T No EVA
rs482147519 35 A>S No EVA
rs446821575 38 D>E No EVA
rs475419969 38 D>G No EVA
rs461428786 38 D>H No EVA
rs466835301 39 A>S No EVA
rs477293203 40 R>G No EVA
rs445886010 40 R>P No EVA
rs437779973 41 A>D No EVA
rs437779973 41 A>G No EVA
rs469134921 41 A>P No EVA
rs454653383 42 V>A No EVA
rs454653383 42 V>G No EVA
rs468294364 43 I>L No EVA
rs433611693 43 I>S No EVA
rs453647169 44 T>P No EVA
rs439037603 46 R>G No EVA
rs475848537 47 V>A No EVA
rs475848537 47 V>G No EVA
rs452607722 47 V>L No EVA
rs444594021 48 S>A No EVA
rs461445952 49 L>H No EVA
rs475088414 50 L>Q No EVA
rs440397085 51 D>E No EVA
rs460527192 55 V>A No EVA
rs477313734 57 V>A No EVA
rs477313734 57 V>G No EVA
rs462831978 58 D>A No EVA
rs462831978 58 D>V No EVA
rs448258763 60 P>A No EVA
rs468904752 171 L>I No EVA
rs472882551 184 V>M No EVA
rs437699337 206 K>I No EVA
rs442759270 218 T>A No EVA
rs459535149 228 E>D No EVA
rs479668672 229 M>I No EVA
rs435308658 293 K>E No EVA
rs455338481 296 E>A No EVA
rs440495416 306 P>T No EVA
rs43308103 316 A>D No EVA
rs434338961 332 N>K No EVA
rs454439023 338 F>L No EVA
rs471263726 343 S>A No EVA
rs438328889 350 K>R No EVA
rs451688723 357 K>Q No EVA
rs443563778 360 K>T No EVA
rs463690319 363 R>K No EVA
rs474137490 367 F>L No EVA
rs380543179 370 R>K No EVA
rs380543179 370 R>M No EVA
rs459522579 372 S>R No EVA
rs135485635 427 V>G No EVA
rs136178223 428 E>G No EVA
rs479075096 456 N>T No EVA
rs463004881 459 D>G No EVA
rs483042819 460 T>R No EVA
rs110344076 487 A>V No EVA

No associated diseases with Q58CU2

No regional properties for Q58CU2

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q58CU2

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell junction, adherens junction
  • Cell membrane ; Peripheral membrane protein
  • Photoreceptor inner segment
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 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.
photoreceptor inner segment The inner segment of a vertebrate photoreceptor containing mitochondria, ribosomes and membranes where opsin molecules are assembled and passed to be part of the outer segment discs.
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
cytoskeletal protein binding Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).

1 GO annotations of biological process

Name Definition
actomyosin structure organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9N179 EPB41 Protein 4.1 Bos taurus (Bovine) PR
Q9MYU8 EPB41L5 Band 4.1-like protein 5 Canis lupus familiaris (Dog) (Canis familiaris) PR
Q9HCS5 EPB41L4A Band 4.1-like protein 4A Homo sapiens (Human) PR
A2A2Y4 FRMD3 FERM domain-containing protein 3 Homo sapiens (Human) PR
Q7Z6J6 FRMD5 FERM domain-containing protein 5 Homo sapiens (Human) PR
Q9HCM4 EPB41L5 Band 4.1-like protein 5 Homo sapiens (Human) PR
P52963 Epb41l4a Band 4.1-like protein 4A Mus musculus (Mouse) PR
Q8BHD4 Frmd3 FERM domain-containing protein 3 Mus musculus (Mouse) PR
Q6P5H6 Frmd5 FERM domain-containing protein 5 Mus musculus (Mouse) PR
Q8BGS1 Epb41l5 Band 4.1-like protein 5 Mus musculus (Mouse) PR
Q0P4Q4 frmd3 FERM domain-containing protein 3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
O57457 epb41l4a Band 4.1-like protein 4 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MLSFFRRTLG RRSMRKQAEK DRLREAQRAA THIPAAGDAR AVITCRVSLL DGTDVSVDLP
70 80 90 100 110 120
KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
130 140 150 160 170 180
KFYSSEPNNL REELTRYLFV LQLKQDILSG KLECPFDTAV QLAAYNLQAE LGDYDLAEHS
190 200 210 220 230 240
PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
250 260 270 280 290 300
DGNDYSLGLT PTGVLVFEGE TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV
310 320 330 340 350 360
FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KNSHRSGFIR LGSRFRYSGK TEYQTTKTNK
370 380 390 400 410 420
ARRSTSFERR PSKRYSRRTL QVKASTGKPE ELSVHNNVSA QSNGSQQAWG VRSTVPVIPS
430 440 450 460 470 480
GPVVVEVENL PKSPGADQHD KKWLSAAGDR SQRGGNQWDT RALSPPHPAP RNYPAFVHEH
490 500
NVKNAGAQQN AHFPGPAAMT DI