Descriptions

Filamins are actin-crosslinking proteins including an N terminal actin-binding domain and 24 Ig-like domain (IgFLNs). The N-terminus of IgFLNa20 forms a β-strand that associates with the integrin binding surface of IgFLNa21 and occupies the binding site for integrin adhesion receptors. Disruption of this IgFLNa20-IgFLNa21 interaction enhances filamin binding to integrin β-tails. In addition, IgFLNa18 negatively regulates the integrin binding to IgFLNa19.

Autoinhibitory domains (AIDs)

Target domain

2046-2141 (IgFLNa19 domain)

Relief mechanism

PTM, Others

Assay

Target domain

2236-2329 (IgFLNa21 domain)

Relief mechanism

PTM, Others

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q80X90

Entry ID Method Resolution Chain Position Source
AF-Q80X90-F1 Predicted AlphaFoldDB

106 variants for Q80X90

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3404848360 13 P>L No EVA
rs3389314324 100 K>R No EVA
rs3389280836 136 A>T No EVA
rs46904175 139 Q>K No EVA
rs3405157719 164 N>G No EVA
rs3405020929 164 N>K No EVA
rs3389280831 201 A>T No EVA
rs3389322832 255 K>N No EVA
rs3389310042 255 K>R No EVA
rs3389314359 330 I>F No EVA
rs3389280818 345 V>M No EVA
rs3389263240 368 G>R No EVA
rs3404821407 399 K>TVLLWLP* No EVA
rs3389310066 416 C>* No EVA
rs3389310057 443 G>D No EVA
rs221221348 444 V>I No EVA
rs3389299665 447 G>W No EVA
rs3389310022 448 E>K No EVA
rs3389291706 487 L>H No EVA
rs3389291713 504 K>* No EVA
rs3404843629 513 F>I No EVA
rs3404821368 516 Y>D No EVA
rs226493499 632 Y>F No EVA
rs3389314313 640 T>I No EVA
rs3389310249 650 A>V No EVA
rs3389310035 717 T>S No EVA
rs3389310193 720 V>M No EVA
rs3389322807 813 P>S No EVA
rs3389234057 815 A>V No EVA
rs3389299717 846 S>N No EVA
rs3389310255 854 G>W No EVA
rs3389304363 861 E>* No EVA
rs3389309035 879 P>Q No EVA
rs220292042 881 N>D No EVA
rs47677451 881 N>I No EVA
rs3389304401 889 P>S No EVA
rs3389273873 891 E>K No EVA
rs240495296 913 T>A No EVA
rs3389309033 924 Y>* No EVA
rs3389299657 929 I>V No EVA
rs3389307222 930 P>H No EVA
rs3389291717 931 K>N No EVA
rs3389291640 936 V>A No EVA
rs217001969 997 A>P No EVA
rs3389299670 1057 K>* No EVA
rs3389299723 1082 E>D No EVA
rs3389322763 1148 V>M No EVA
rs3389307225 1159 S>* No EVA
rs49448575 1181 S>T No EVA
rs3389309027 1243 V>M No EVA
rs3389309054 1259 T>S No EVA
rs3389291637 1261 V>D No EVA
rs3389307180 1270 I>N No EVA
rs3389291663 1279 E>* No EVA
rs3389280860 1286 A>V No EVA
rs3389280826 1309 D>V No EVA
rs3389304410 1366 E>K No EVA
rs3389291697 1367 G>W No EVA
rs3389307210 1394 D>N No EVA
rs3389314404 1434 C>R No EVA
rs3389263278 1435 V>I No EVA
rs3550730455 1458 R>K No EVA
rs3389319317 1478 T>I No EVA
rs3404843627 1489 G>R No EVA
rs3412537096 1490 P>S No EVA
rs3389309071 1525 P>S No EVA
rs3389273839 1542 I>V No EVA
rs3389307182 1548 G>D No EVA
rs3389309032 1629 K>R No EVA
rs3389310264 1631 G>D No EVA
rs3389291662 1687 Y>* No EVA
rs3389307175 1691 G>C No EVA
rs250737167 1712 M>V No EVA
rs3389280871 1721 P>S No EVA
rs3389319321 1735 P>H No EVA
rs3389306797 1745 K>N No EVA
rs3389322790 1760 I>F No EVA
rs3389319294 1798 M>K No EVA
rs3389304152 1830 G>D No EVA
rs3389314395 1874 G>W No EVA
rs3389310010 1905 T>A No EVA
rs3389310237 1953 L>M No EVA
rs3389304087 1995 V>I No EVA
rs3389304277 2019 E>D No EVA
rs3389306823 2065 V>M No EVA
rs3389304395 2123 E>* No EVA
rs3389291684 2176 V>E No EVA
rs3404839182 2181 F>L No EVA
rs3404956630 2183 F>S No EVA
rs3404900823 2183 F>V No EVA
rs3389319255 2232 G>S No EVA
rs46270299 2260 Y>* No EVA
rs3389305802 2281 I>F No EVA
rs3412926966 2293 L>M No EVA
rs3389291709 2305 P>S No EVA
rs3389302241 2313 N>I No EVA
rs3389319332 2365 H>L No EVA
rs3389310199 2368 G>R No EVA
rs3389273882 2399 T>A No EVA
rs3389263234 2448 G>R No EVA
rs3550685140 2493 V>I No EVA
rs3389299671 2566 K>R No EVA
rs3389304135 2569 Y>F No EVA
rs864286217 2573 Y>N No EVA
rs3389263249 2583 L>M No EVA
rs3389299643 2589 E>K No EVA

No associated diseases with Q80X90

3 regional properties for Q80X90

Type Name Position InterPro Accession
domain Lactate/malate dehydrogenase, N-terminal 88 - 235 IPR001236
active_site Malate dehydrogenase, active site 237 - 249 IPR001252
domain Lactate/malate dehydrogenase, C-terminal 238 - 408 IPR022383

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cell cortex
  • Cytoplasm, cytoskeleton
  • Cytoplasm, cytoskeleton, stress fiber
  • Cytoplasm, myofibril, sarcomere, Z line
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 GO annotations of cellular component

Name Definition
brush border The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
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.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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).
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
phagocytic vesicle A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
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.
Z disc Platelike region of a muscle sarcomere to which the plus ends of actin filaments are attached.

2 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.
identical protein binding Binding to an identical protein or proteins.

5 GO annotations of biological process

Name Definition
actin 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 comprising actin filaments and their associated proteins.
cellular response to type II interferon Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon gamma is the only member of the type II interferon found so far.
epithelial cell morphogenesis The change in form that occurs when an epithelial cell progresses from its initial formation to its mature state.
keratinocyte development The process whose specific outcome is the progression of a keratinocyte over time, from its formation to the mature structure.
skeletal muscle tissue development The developmental sequence of events leading to the formation of adult skeletal muscle tissue. The main events are

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VEN1 cher Filamin-A Drosophila melanogaster (Fruit fly) SS
P21333 FLNA Filamin-A Homo sapiens (Human) SS
O75369 FLNB Filamin-B Homo sapiens (Human) EV
Q8BTM8 Flna Filamin-A Mus musculus (Mouse) SS
10 20 30 40 50 60
MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK
70 80 90 100 110 120
RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH
130 140 150 160 170 180
YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP
190 200 210 220 230 240
GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA
250 260 270 280 290 300
KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
310 320 330 340 350 360
EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK
370 380 390 400 410 420
GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP
430 440 450 460 470 480
VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK
490 500 510 520 530 540
AAGSGELGVT VKGPKGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE
550 560 570 580 590 600
VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN
610 620 630 640 650 660
DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC
670 680 690 700 710 720
TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV
730 740 750 760 770 780
VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG
790 800 810 820 830 840
IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD
850 860 870 880 890 900
PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL NVQFSSPLPG EAVKDLDIID
910 920 930 940 950 960
NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK
970 980 990 1000 1010 1020
DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY
1030 1040 1050 1060 1070 1080
DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP
1090 1100 1110 1120 1130 1140
CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG
1150 1160 1170 1180 1190 1200
PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG
1210 1220 1230 1240 1250 1260
MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ
1270 1280 1290 1300 1310 1320
VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV
1330 1340 1350 1360 1370 1380
AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD
1390 1400 1410 1420 1430 1440
GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP
1450 1460 1470 1480 1490 1500
QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE
1510 1520 1530 1540 1550 1560
EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE
1570 1580 1590 1600 1610 1620
GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT
1630 1640 1650 1660 1670 1680
GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK
1690 1700 1710 1720 1730 1740
PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN
1750 1760 1770 1780 1790 1800
GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI
1810 1820 1830 1840 1850 1860
KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG
1870 1880 1890 1900 1910 1920
PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL
1930 1940 1950 1960 1970 1980
GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK
1990 2000 2010 2020 2030 2040
NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE
2050 2060 2070 2080 2090 2100
GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT
2110 2120 2130 2140 2150 2160
RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ
2170 2180 2190 2200 2210 2220
EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE
2230 2240 2250 2260 2270 2280
AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV
2290 2300 2310 2320 2330 2340
IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP
2350 2360 2370 2380 2390 2400
DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG
2410 2420 2430 2440 2450 2460
IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN
2470 2480 2490 2500 2510 2520
HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA
2530 2540 2550 2560 2570 2580
GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD
2590 2600
YVLAVKWGEE HIPGSPFHVT VP