ID A0A1V4KF14_PATFA Unreviewed; 891 AA.
AC A0A1V4KF14;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=ACTN1 {ECO:0000313|EMBL:OPJ83060.1};
GN ORFNames=AV530_010487 {ECO:0000313|EMBL:OPJ83060.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ83060.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ83060.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ83060.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ83060.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OPJ83060.1}.
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DR EMBL; LSYS01003385; OPJ83060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KF14; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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; IPR018247; EF_Hand_1_Ca_BS.
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; PF13405; EF-hand_6; 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; 3.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
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:UP000190648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 30..134
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 143..249
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 745..780
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 786..821
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 264..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 429..463
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 891 AA; 102918 MW; 679FE81E226191DE CRC64;
MDHYDQQTND YMQPEEDWDR DLLLDPAWEK QQRKTFTAWC NSHLRKAGTQ IENIEEDFRD
GLKLMLLLEV ISGERLAKPE RGKMRVHKIS NVNKALDFIA SKGVKLVSIG AEEIVDGNVK
MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY KNVNIQNFHI SWKDGLGFCA
LIHRHRPELI DYGKLRKDDP LTNLNTAFDV AEKYLDIPKM LDAEDIVGTA RPDEKAIMTY
VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEQLMEDYEK LASDLLEWIR RTIPWLENRA
PENTMQAMQQ KLEDFRDYRR LHKPPKVQEK CQLEINFNTL QTKLRLSNRP AFMPSEGKMV
SDINNAWGGL EQAEKGYEEW LLNEIRRLER LDHLAEKFRQ KASIHESWTD GKEAMLQQKD
YETATLSEIK ALLKKHEAFE SDLAAHQDRV EQIAAIAQEL NELDYYDSPS VNARCQKICD
QWDNLGALTQ KRREALERTE KLLETIDQLY LEYAKRAAPF NNWMEGAMED LQDTFIVHTI
EEIQGLTTAH EQFKATLPDA DKERQAILGI HNEVSKIVQT YHVNMAGTNP YTTITPHEIN
GKWEHVRQLV PRRDQALMEE HARQQQNERL RKQFGAQANV IGPWIQTKME EIGRISIEMH
GTLEDQLNHL RQYEKSIVNY KPKIDQLEGD HQQIQEALIF DNKHTNYTME HIRVGWEQLL
TTIARTINEV ENQILTRDAK GISQEQMNEF RASFNHFDRD HSGTLGPEEF KACLISLGYD
IGNDAQGEAE FARIMSIVDP NRLGVVTFQA FIDFMSRETA DTDTADQVMA SFKILAGDKN
YITVDELRRE LPPDQAEYCI ARMAPYNGRD AVPGALDYMS FSTALYGESD L
//
