Descriptions

Importin-α is a nuclear import receptor that facilitates the transport of proteins with nuclear localization sequences (NLSs) into the nucleus. It is autoinhibited by its N-terminal region, which occupies the NLS-binding site, preventing unnecessary binding and import activity. Importin-α is autoinhibited in the absence of importin-β and the binding of importin-β alleviates this autoinhibition, which displaces the autoinhibitory sequence.

Autoinhibitory domains (AIDs)

Target domain

588-684 (F3 subdomain)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

0 structures for F1Q8X5

Entry ID Method Resolution Chain Position Source
No available structures

No variants for F1Q8X5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F1Q8X5

No associated diseases with F1Q8X5

9 regional properties for F1Q8X5

Type Name Position InterPro Accession
repeat Armadillo 92 - 175 IPR000225-1
repeat Armadillo 176 - 218 IPR000225-2
repeat Armadillo 220 - 259 IPR000225-3
repeat Armadillo 261 - 301 IPR000225-4
repeat Armadillo 303 - 344 IPR000225-5
repeat Armadillo 346 - 386 IPR000225-6
repeat Armadillo 389 - 429 IPR000225-7
domain Importin-alpha, importin-beta-binding domain 1 - 70 IPR002652
repeat Atypical Arm repeat 451 - 500 IPR032413

Functions

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

9 GO annotations of cellular component

Name Definition
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
cell surface The external part of the cell wall and/or plasma membrane.
extrinsic component of cytoplasmic side of plasma membrane The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
I band A region of a sarcomere that appears as a light band on each side of the Z disc, comprising a region of the sarcomere where thin (actin) filaments are not overlapped by thick (myosin) filaments; contains actin, troponin, and tropomyosin; each sarcomere includes half of an I band at each end.
intercalated disc A complex cell-cell junction at which myofibrils terminate in cardiomyocytes; mediates mechanical and electrochemical integration between individual cardiomyocytes. The intercalated disc contains regions of tight mechanical attachment (fasciae adherentes and desmosomes) and electrical coupling (gap junctions) between adjacent cells.
lamellipodium membrane The portion of the plasma membrane surrounding a lamellipodium.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
stress fiber A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.

2 GO annotations of molecular function

Name Definition
integrin binding Binding to an integrin.
lipid binding Binding to a lipid.

8 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
cardiac muscle tissue morphogenesis The process in which the anatomical structures of cardiac muscle tissue are generated and organized.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues.
cell-matrix adhesion The binding of a cell to the extracellular matrix via adhesion molecules.
cytoskeleton 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.
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.
regulation of cell shape Any process that modulates the surface configuration of a cell.
Wnt signaling pathway The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q32LP0 FERMT3 Fermitin family homolog 3 Bos taurus (Bovine) SS
Q9VZI3 Fit1 Unc-112-related protein Drosophila melanogaster (Fruit fly) 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
10 20 30 40 50 60
MKGGETMSVR RSGYKAVVDG VGGRRRREDD MVEIRKAKRE ESLLKKRREA LPHSPSADSL
70 80 90 100 110 120
DQKLISCIWS DERDLLIEAT TQIRTLLCGE MFNVRVEEVI QAGLVPRFVE FLTWDDSPQL
130 140 150 160 170 180
QFEAAWALTN IASGTSENTE VVIDHGAVAI LVRLLNSPYD VVREQVVWAL GNISGDSPRC
190 200 210 220 230 240
RDIVLGHAAL PSLLLQLNHG AKLSMLVNAA WTLSNLCRGK PQPPFDQVSA ALPALAQLIR
250 260 270 280 290 300
LDDKELLAYT CWALVYLSDG SNEKIQAVIE ANVCARLIGL SIHRSPSVIT PALRTIGNIV
310 320 330 340 350 360
TGNDSQTQHI IDLQALPCLV NLLRGSYNKT IRKEACWTVS NITAGCQSQI QAVFDADICP
370 380 390 400 410 420
ALVNLLQNSE GDVKKEAAWA ICNAIAGGSY KQIMFLVKQE CIKPLCDLLT CSDTQLVMVC
430 440 450 460 470 480
LEALKKILKV GEVFSSRHAE GIYQCPQTNV NPHAQLIEEA EGLEKIEGLQ SHENNDIYET
490 500 510 520
AVKILETYWM EEEEEEDQEQ QDMIYFPVDN FANMPTSSGT LSEMHCGP