Q9VZI3

SS
Gene name
Fit1 (CG14991)
Protein name
Unc-112-related protein
Names
Fermitin-1
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG14991
EC number
Protein Class

Descriptions

Kindlin-3 is a member of the kindlin family of focal adhesion proteins which bind to integrin beta-chain cytoplasmic domains to regulate integrin function. kindlin-3 is maintained in a homotrimer state, which is different from the monomer that binds integrin β cytoplasmic tails. The trimer formation of kindlin-3 results in an autoinhibited state, as the integrin-binding pocket is blocked by the pleckstrin homology (PH) domain of another protomer. Mutations disrupting the trimer interface (Q471A, A475F, S478A) lead to increased integrin-mediated cell adhesion and spreading, indicating relief from autoinhibition. This autoinhibition regulates kindlin-3’s role in integrin activation and signaling, with implications for diseases like leukocyte adhesion deficiency (LAD) III and cancer.

Autoinhibitory domains (AIDs)

415-544 (PH domain) SS

Target domain

613-708 (F3 subdomain)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9VZI3

Entry ID Method Resolution Chain Position Source
AF-Q9VZI3-F1 Predicted AlphaFoldDB

No variants for Q9VZI3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VZI3

No associated diseases with Q9VZI3

5 regional properties for Q9VZI3

Type Name Position InterPro Accession
domain Pleckstrin homology domain 400 - 510 IPR001849
domain FERM central domain 305 - 602 IPR019748
domain Band 4.1 domain 83 - 602 IPR019749
domain Kindlin/fermitin, PH domain 401 - 529 IPR037837
domain Kindlin-2, N-terminal 4 - 87 IPR040790

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cell-substrate junction A cell junction that forms a connection between a cell and the extracellular matrix.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
cell adhesion molecule binding Binding to a cell adhesion molecule.
integrin binding Binding to an integrin.

4 GO annotations of biological process

Name Definition
cardiac muscle tissue development The process whose specific outcome is the progression of cardiac muscle over time, from its formation to the mature structure.
cell-matrix adhesion The binding of a cell to the extracellular matrix via adhesion molecules.
defense response to Gram-negative bacterium Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.
integrin-mediated signaling pathway The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q32LP0 FERMT3 Fermitin family homolog 3 Bos taurus (Bovine) SS
Q86UX7 FERMT3 Fermitin family homolog 3 Homo sapiens (Human) EV
Q9BQL6 FERMT1 Fermitin family homolog 1 Homo sapiens (Human) SS
Q96AC1 FERMT2 Fermitin family homolog 2 Homo sapiens (Human) SS
Q9Y4G6 TLN2 Talin-2 Homo sapiens (Human) SS
Q9Y490 TLN1 Talin-1 Homo sapiens (Human) EV
P59113 Fermt1 Fermitin family homolog 1 Mus musculus (Mouse) SS
Q8CIB5 Fermt2 Fermitin family homolog 2 Mus musculus (Mouse) SS
Q8K1B8 Fermt3 Fermitin family homolog 3 Mus musculus (Mouse) SS
P26039 Tln1 Talin-1 Mus musculus (Mouse) EV
Q18685 unc-112 Protein unc-112 Caenorhabditis elegans SS
F1Q8X5 fermt2 Fermitin family homolog 2 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MIHVGENTWN LRILITDLQV EKTLRVKGDQ HIGGVMLNLV DPELPKDWSD HALWWPAKNI
70 80 90 100 110 120
WLTRTRSTLD QAGVQSDSFL HFTPMHKTLR VQMPDLRYLD YRVNFSAKTF GAVVSLCKDL
130 140 150 160 170 180
DIRYPEELSF CKPLEPEHLK KNFSKLPQRK IPVAEANGIA YVQPALDTNS FVPITGAYNG
190 200 210 220 230 240
SNGSLDRSHN GNLLCAPASP YTRRAATAPG TPISSPTGTW KHNSTGYASY DSNSSFGDLQ
250 260 270 280 290 300
ENLAMSPRSP SPDVRARLVR PKSRVEKARL NVGWLDSSLS IMEQGVREYD TLCLRFKYFT
310 320 330 340 350 360
FFDLNPKYDQ VRINQLYEQA KWSILNEELE PTEEETLMFA ALQFQVNHQT DLHPPGIDSG
370 380 390 400 410 420
IDTSSQETGG EDDIDSALNE LQITLEGPGG GKDQGNITRI PELSDYLKFL KPQRFTLKGY
430 440 450 460 470 480
KRYFFTYRDL HLHLYKSQDE SRRGAPTISI NLKGCEVTPD VNLAQGKFAI RLEVPSEIRN
490 500 510 520 530 540
GPNSEVWVRC DNEEQYAKWM AACRLAAKGR SLADSSYDSE VSSIRSLLQM QKPAQGAPLT
550 560 570 580 590 600
VNPRSVEPMD YLSPKMMRKL SSKAVQRILE AHANVRQLSL MDAKMKYIQA WQSLPDFGVT
610 620 630 640 650 660
LFIIKFDGHK KEELLGVANN RIMRMDLNTG DHIKTWRYNT MKAWNVNWGI KCMMIQLQDE
670 680 690 700
NIVFSVQSAD CKVVHEFIGG YIFMSMRSKE NNQTLNEEMF HKLTGGWS