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Database: UniProt
Entry: A0A3L8SXV5_CHLGU
LinkDB: A0A3L8SXV5_CHLGU
Original site: A0A3L8SXV5_CHLGU 
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
//
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