ID A0A3L8SXV5_CHLGU Unreviewed; 1121 AA.
AC A0A3L8SXV5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Alpha-actinin-1 {ECO:0000256|ARBA:ARBA00018384};
DE AltName: Full=Alpha-actinin cytoskeletal isoform {ECO:0000256|ARBA:ARBA00041477};
DE AltName: Full=F-actin cross-linking protein {ECO:0000256|ARBA:ARBA00043249};
DE AltName: Full=Non-muscle alpha-actinin-1 {ECO:0000256|ARBA:ARBA00042871};
GN ORFNames=DV515_00002223 {ECO:0000313|EMBL:RLW10342.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW10342.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW10342.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW10342.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW10342.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000256|ARBA:ARBA00004216}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW10342.1}.
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DR EMBL; QUSF01000004; RLW10342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SXV5; -.
DR STRING; 44316.ENSEGOP00005001237; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd21216; CH_ACTN_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 2.
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:SF434; ALPHA-ACTININ-1; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
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; 3.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 221..325
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 334..440
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 980..1015
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1016..1051
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 664..698
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1121 AA; 128785 MW; 9629F5CCF1998D7C CRC64;
MDHYDAQQTN DYMQPEEDWD RDLLLDPAWE KQQRKGESWL LEYDAEEKHW FRTSSYLHLP
GRLLFYSVGA GKGNVFPSYS AIVFSDLTCF GLKIAVLLRG DSSKHQAEDK RLVQDLPVLC
MQAQHEQSAL TVMAIVLVLS SPLVYIPEER FPCEESIVSM EKISQELGKK EERCKLHLVS
RGGMIPSGEQ GQSTAVEGLA AVEQCFFQGN VLPHYMWSVE LKWEQTFTAW CNSHLRKAGT
QIENIEEDFR DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI
GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH
ISWKDGLGFC ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT
ARPDEKAIMT YVSSFYHAFS GAQKVSQDSK LPPQSTPDII GTLRPDEKAI MTYVSCYYHA
FSGAQKAETA ANRICKVLAV NQENEQLMED YEKLASDVGL LEWIRRTIPW LENRAPENTM
QAMQQKLEDF RDYRRLHKPP KVQEKCQLEI NFNTLQTKLR LSNRPAFMPS EGKMVSDINN
AWGGLEQAEK GYEEWLLNEI RRLERLDHLA EKFRQKASIH ESWTDGKEAM LQQKDYETAT
LSEIKALLKK HEAFESDLAA HQDRVEQIAA IAQELNELDY YDSPSVNARC QKICDQWDNL
GALTQKRREA LERTEKLLET IDQLYLEYAK RAAPFNNWME GAMEDLQDTF IVHTIEEIQG
LTTAHEQFKA TLPDADKERQ AILGIHNEVS KIVQTYHVNM AGTNPYTTIT PHEINGKWEH
VRQLVPRRDQ ALMEEHARQQ QNERLRKQFG AQANVIGPWI QTKMEEIGRI SIEMHGTLED
QLNHLRQYEK SIVNYKPKID QLEGDHQLIQ EALIFDNKHT NYTMEHIRVG WEQLLTTIAR
TINEVENQIL TRDAKGISQE QMNEFRASFN HFDRKKTGMM DCEDFRACLI SMGYNMGEAE
FARIMSIVDP NRLGVVTFQA FIDFMSRETA DTDTADQVMA SFKILAGDKN YITVDELRRE
LPPDQAEYCI ARMAPYNGRD AVPGALDYMS FSTALYGESD L
//