P20111

SS
Gene name
ACTN2
Protein name
Alpha-actinin-2
Names
Alpha-actinin skeletal muscle isoform 2, F-actin cross-linking protein
Species
Gallus gallus (Chicken)
KEGG Pathway
gga:396263
EC number
Protein Class

Descriptions

ACTN2 is F-actin cross-linking protein. Interaction with the Z-repeat of Titin protein via the C-terminal region of ACTN2 targets ACTN2 to Z-disk. Full-length ACTN2 does not bind Z-repeats. ACTN2 has a region between ABD and R1 acting as a pseudo-Z-repeat, and this region prevents the binding of ACTN2 to the Z-repeat of Titin protein.

Autoinhibitory domains (AIDs)

262-310 (Pseudo-Z-repeat) SS

Target domain

756-893 (EF-hand domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P20111

Entry ID Method Resolution Chain Position Source
AF-P20111-F1 Predicted AlphaFoldDB

4 variants for P20111

Variant ID(s) Position Change Description Diseaes Association Provenance
rs733538264 329 Y>S No Ensembl
rs740467351 467 I>M No Ensembl
rs732823426 639 E>D No Ensembl
rs317911698 898 L>W No Ensembl

No associated diseases with P20111

7 regional properties for P20111

Type Name Position InterPro Accession
domain Cyclic nucleotide-binding domain 136 - 252 IPR000595-1
domain Cyclic nucleotide-binding domain 254 - 375 IPR000595-2
domain cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain 24 - 61 IPR003117
conserved_site Cyclic nucleotide-binding, conserved site 163 - 179 IPR018488-1
conserved_site Cyclic nucleotide-binding, conserved site 199 - 216 IPR018488-2
conserved_site Cyclic nucleotide-binding, conserved site 281 - 297 IPR018488-3
conserved_site Cyclic nucleotide-binding, conserved site 323 - 340 IPR018488-4

Functions

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

2 GO annotations of cellular component

Name Definition
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
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 binding Binding to monomeric or multimeric forms of actin, including actin filaments.
calcium ion binding Binding to a calcium ion (Ca2+).

1 GO annotations of biological process

Name Definition
microspike assembly Formation of a microspike, a dynamic, actin-rich projection extending from the surface of a migrating animal cell.

17 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A5D7D1 ACTN4 Alpha-actinin-4 Bos taurus (Bovine) SS
Q0III9 ACTN3 Alpha-actinin-3 Bos taurus (Bovine) SS
Q3B7N2 ACTN1 Alpha-actinin-1 Bos taurus (Bovine) SS
Q3ZC55 ACTN2 Alpha-actinin-2 Bos taurus (Bovine) SS
P05094 ACTN1 Alpha-actinin-1 Gallus gallus (Chicken) SS
Q90734 ACTN4 Alpha-actinin-4 Gallus gallus (Chicken) SS
P18091 Actn Alpha-actinin, sarcomeric Drosophila melanogaster (Fruit fly) SS
Q08043 ACTN3 Alpha-actinin-3 Homo sapiens (Human) SS
O43707 ACTN4 Alpha-actinin-4 Homo sapiens (Human) SS
P12814 ACTN1 Alpha-actinin-1 Homo sapiens (Human) SS
P35609 ACTN2 Alpha-actinin-2 Homo sapiens (Human) EV
O88990 Actn3 Alpha-actinin-3 Mus musculus (Mouse) SS
P57780 Actn4 Alpha-actinin-4 Mus musculus (Mouse) SS
Q7TPR4 Actn1 Alpha-actinin-1 Mus musculus (Mouse) SS
Q9JI91 Actn2 Alpha-actinin-2 Mus musculus (Mouse) SS
Q9Z1P2 Actn1 Alpha-actinin-1 Rattus norvegicus (Rat) SS
Q9QXQ0 Actn4 Alpha-actinin-4 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MNSMNQIETN MQYTYNYEED EYMTQEEEWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT
70 80 90 100 110 120
QIENIEEDFR NGLKLMLLLE VISGERLPKP DRGKMRFHKI ANVNKALDYI ASKGVKLVSI
130 140 150 160 170 180
GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YRNVNIQNFH
190 200 210 220 230 240
LSWKDGLGLC ALIHRHRPDL IDYSKLNKDD PIGNINLAME IAEKHLDIPK MLDAEDIVNT
250 260 270 280 290 300
PKPDERAIMT YVSCFYHAFA GAEQAETAAN RICKVLAVNQ ENERLMEEYE RLASELLEWI
310 320 330 340 350 360
RRTIPWLENR TPEKTMQAMQ KKLEDFRDYR RKHKPPKVQE KCQLEINFNT LQTKLRISNR
370 380 390 400 410 420
PAFMPSEGKM VSDIAGAWQR LEQAEKGYEE WLLNEIRRLE RLEHLAEKFR QKASTHEQWA
430 440 450 460 470 480
YGKEQILLQK DYESASLTEV RAMLRKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYHDAA
490 500 510 520 530 540
SVNDRCQKIC DQWDSLGTLT QKRREALERT EKLLETIDQL HLEFAKRAAP FNNWMEGAME
550 560 570 580 590 600
DLQDMFIVHS IEEIQSLISA HDQFKATLPE ADGERQAILS IQNEVEKVIQ SYSMRISASN
610 620 630 640 650 660
PYSTVTVEEI RTKWEKVKQL VPQRDQSLQE ELARQHANER LRRQFAAQAN VIGPWIQTKM
670 680 690 700 710 720
EEIARSSIEM TGPLEDQMNQ LKQYEQNIIN YKHNIDKLEG DHQLIQEALV FDNKHTNYTM
730 740 750 760 770 780
EHIRVGWELL LTTIARTINE VETQILTRDA KGITQEQMND FRASFNHFDR RKNGLMDHDD
790 800 810 820 830 840
FRACLISMGY DLGEAEFARI MSLVDPNGQG TVTFQSFIDF MTRETADTDT AEQVIASFRI
850 860 870 880 890
LASDKPYILA DELRRELPPE QAQYCIKRMP QYTGPGSVPG ALDYTSFSSA LYGESDL