Q3MHM6

SS
Gene name
CTNNA1
Protein name
Catenin alpha-1
Names
Species
Bos taurus (Bovine)
KEGG Pathway
bta:526848
EC number
Protein Class

Descriptions

Alpha-catenin acts as a mechanosensor in adherens junction formation by facilitating the recruitment of vinculin to adherens junctions in the actomyosin-derived tension-dependent manner. Alpha-catenin consists of three major domains with distinct functionalities: an N-terminal (N) domain participates in beta-catenin binding and homodimerization; a modulatory (M) domain interacts with several actin-binding proteins, including vinculin; and a C-terminal (C) domain directly and/or indirectly binds to F-actin. In catenin alpha-1 (Ctnna1, αE-catenin), the vinculin-binding site (VBS) is autoinhibited by occluding the vinculin-binding hydrophobic surfaces within the MI helical bundle. The MIII region inhibits the interaction between the VBS and vinculin. In the high-tension state, Ctnna1 adopts the "open" conformation that disrupts the inhibitory role of MIII region, releasing the MI bundle and unfurling the vinculin-binding site.

Autoinhibitory domains (AIDs)

507-631 (MIII domain) SS

Target domain

305-352 (vinculin-binding site within the MI region)

Relief mechanism

Others

Assay

636-650 (M-FABD linker) SS

Target domain

669-863 (F-actin binding domain)

Relief mechanism

Partner binding

Assay

3-262 (N-terminal region) SS

Target domain

263-631 (Middle region)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q3MHM6

Entry ID Method Resolution Chain Position Source
AF-Q3MHM6-F1 Predicted AlphaFoldDB

No variants for Q3MHM6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3MHM6

No associated diseases with Q3MHM6

3 regional properties for Q3MHM6

Type Name Position InterPro Accession
domain Interferon regulatory factor, DNA-binding domain 3 - 115 IPR001346
domain Interferon regulatory factor-3 202 - 380 IPR019471
conserved_site Interferon regulatory factor, conserved site 28 - 61 IPR019817

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cell junction, adherens junction
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell junction
  • Cytoplasm
  • Nucleus
  • Found only at cell-cell boundaries
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
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.
catenin complex Complex of peripheral cytoplasmic proteins (alpha-, beta- and gamma-catenin) that interact with the cytoplasmic region of uvomorulin/E-cadherin to connect it to the actin cytoskeleton.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
beta-catenin binding Binding to a catenin beta subunit.
cadherin binding Binding to cadherin, a type I membrane protein involved in cell adhesion.
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex.

3 GO annotations of biological process

Name Definition
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues.
cell-cell adhesion The attachment of one cell to another cell via adhesion molecules.
negative regulation of protein localization to nucleus Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to nucleus.

16 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P12003 VCL Vinculin Gallus gallus (Chicken) EV
P30997 CTNNA2 Catenin alpha-2 Gallus gallus (Chicken) SS
P35220 alpha-Cat Catenin alpha Drosophila melanogaster (Fruit fly) SS
P18206 VCL Vinculin Homo sapiens (Human) SS
P26232 CTNNA2 Catenin alpha-2 Homo sapiens (Human) SS
Q9UI47 CTNNA3 Catenin alpha-3 Homo sapiens (Human) SS
P35221 CTNNA1 Catenin alpha-1 Homo sapiens (Human) EV
Q64727 Vcl Vinculin Mus musculus (Mouse) SS
Q65CL1 Ctnna3 Catenin alpha-3 Mus musculus (Mouse) EV
Q61301 Ctnna2 Catenin alpha-2 Mus musculus (Mouse) EV
P26231 Ctnna1 Catenin alpha-1 Mus musculus (Mouse) EV
P26234 VCL Vinculin Sus scrofa (Pig) SS
P85972 Vcl Vinculin Rattus norvegicus (Rat) SS
P90947 hmp-1 Alpha-catenin-like protein hmp-1 Caenorhabditis elegans SS
A4IGI7 ctnna2 Catenin alpha-2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) SS
B7ZC77 Ctnna2 Catenin alpha-2 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MTAVHTGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
70 80 90 100 110 120
LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ CDLMKSAAGE FADDPCSSVK
130 140 150 160 170 180
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKLVEDG ILKLRNAGTE QDLGIQYKAL
190 200 210 220 230 240
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
250 260 270 280 290 300
RDLIYKQLQQ AVTGISNAAQ ATASDDASQH PGAGGGELAY ALNNFDKQII VDPLSFSEER
310 320 330 340 350 360
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
370 380 390 400 410 420
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLVEAAKN GNEKEVKEYA
430 440 450 460 470 480
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
490 500 510 520 530 540
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
550 560 570 580 590 600
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
610 620 630 640 650 660
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
670 680 690 700 710 720
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
730 740 750 760 770 780
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL
790 800 810 820 830 840
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
850 860 870 880 890 900
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
KAMDSI