ID U3KG99_FICAL Unreviewed; 897 AA.
AC U3KG99;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Actinin alpha 2 {ECO:0000313|Ensembl:ENSFALP00000014053.1};
GN Name=ACTN2 {ECO:0000313|Ensembl:ENSFALP00000014053.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000014053.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000014053.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000014053.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR RefSeq; XP_016152808.1; XM_016297322.1.
DR STRING; 59894.ENSFALP00000014053; -.
DR Ensembl; ENSFALT00000014111.2; ENSFALP00000014053.1; ENSFALG00000013451.2.
DR Ensembl; ENSFALT00000014113.2; ENSFALP00000014055.1; ENSFALG00000013451.2.
DR GeneID; 101811963; -.
DR CTD; 88; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000153968; -.
DR HOGENOM; CLU_005217_1_1_1; -.
DR OMA; VRYDNGY; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000016665; Chromosome 3.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051373; F:FATZ binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030274; F:LIM domain binding; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0031432; F:titin binding; IEA:Ensembl.
DR GO; GO:0070080; F:titin Z domain binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0051695; P:actin filament uncapping; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0030035; P:microspike assembly; IEA:Ensembl.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; IEA:Ensembl.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IEA:Ensembl.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR CDD; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd21216; CH_ACTN_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 1.20.58.60; -; 4.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF429; ALPHA-ACTININ-2; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00150; SPEC; 2.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 41..145
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 154..260
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 756..791
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 792..827
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 275..302
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 674..701
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 897 AA; 104254 MW; 7E716CE152D23810 CRC64;
MNSMNQIDTN MQYTYNYEED EYMTQEEEWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT
QIENIEEDFR NGLKLMLLLE VISGERLPKP DRGKMRFHKI ANVNKALDYI ASKGVKLVSI
GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YRNVNIQNFH
LSWKDGLGLC ALIHRHRPDL IDYSKLNKDD PIGNINLAME IAEKHLDIPK MLDAEDIVNT
PKPDERAIMT YVSCFYHAFA GAEQAETAAN RICKVLAVNQ ENERLMEEYE RLASELLEWI
RRTIPWLENR TPEKTMQAMQ KKLEDFRDYR RKHKPPKVQE KCQLEINFNT LQTKLRISNR
PAFMPSEGKM VSDIAGAWQR LEQAEKGYEE WLLNEIRRLE RLEHLAEKFR QKASTHEQWA
YGKEQTLLQK DYESASLTEV RAMLRKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYHDAA
SVNDRCQKIC DQWDSLGTLT QKRREALERT EKLLETIDQL HLEFAKRAAP FNNWMEGAME
DLQDMFIVHS IEEIQSLISA HDQFKATLPE ADGERQAILS IQNEVEKVIQ SYNMRISATN
PYSTVTVEEI RSKWEKVKQL VPQRDQSLQE ELARQHANER LRRQFAAQAN VIGPWIQTKM
EEIARSSIEM TGPLEDQMNQ LKQYEHNIIN YKHNIDKLEG DHQLIQEALV FDNKHTNYTM
EHIRVGWELL LTTIARTINE VETQILTRDA KGITQEQMND FRASFNHFDR RKNGLMDHDD
FRACLISMGY DLGEAEFARI MSLVDPNGQG TVTFQSFIDF MTRETADTDT AEQVIASFRI
LASDKPYILA DELRRELPPE QAQYCIKRMP PYTGPGSVPG ALDYTSFSSA LYGESDL
//
