ID   W5UL66_ICTPU            Unreviewed;       894 AA.
AC   W5UL66;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Alpha-actinin-2 {ECO:0000313|EMBL:AHH42879.1, ECO:0000313|RefSeq:XP_017332685.1};
GN   Name=Actn2 {ECO:0000313|EMBL:AHH42879.1};
GN   Synonyms=actn2b {ECO:0000313|RefSeq:XP_017332685.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH42879.1};
RN   [1] {ECO:0000313|EMBL:AHH42879.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mixed {ECO:0000313|EMBL:AHH42879.1};
RX   PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA   Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA   Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA   Peatman E., Liu Z.;
RT   "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT   Seq analysis of a doubled haploid homozygote.";
RL   BMC Genomics 13:595-595(2012).
RN   [2] {ECO:0000313|RefSeq:XP_017332685.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017332685.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family.
CC       {ECO:0000256|ARBA:ARBA00010255}.
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DR   EMBL; JT418868; AHH42879.1; -; mRNA.
DR   RefSeq; XP_017332685.1; XM_017477196.3.
DR   STRING; 7998.ENSIPUP00000022215; -.
DR   Ensembl; ENSIPUT00000023167; ENSIPUP00000022215; ENSIPUG00000014923.
DR   GeneID; 108270464; -.
DR   KEGG; ipu:108270464; -.
DR   CTD; 641575; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000221080; Chromosome 9.
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; 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; 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   2: Evidence at transcript level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          38..142
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          151..257
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          753..788
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          789..824
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   894 AA;  103197 MW;  A32B84D62455B107 CRC64;
     MIEMENSVLY DNGFYQEEYM MQEDEWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE
     NIEDDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV NKALDFITSK GVKLVSIGAE
     EIVDGNVKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNVQNFHVSW
     KDGLAFCALI HRHRPDLIDY AKLNKDDPLG NLNLAFDVAE KHLDIPKMLD AEDIVNTPKP
     DERAIMTYVS CFYHAFAGAE QAETAANRIC KLLGVNQENE KLMEDYERLA SELLEWIMRT
     TPWLENRVSE KSVALMQRKL EDFRDYRRLH KPPKVQEKCQ LEINFNTLQT KLRISNRPAF
     MPSEGKMVSD IASAWQGLEQ AEKGYEEWLL TEIRKLLRVD HLAEKFRQKA TTHETWASGK
     EELLIQKDYE SASLMEVRAL LRKHEAFESD LSAHQDRVEQ IAAIAQELNE LDYHDVAAVN
     QRCQSICDVW DKLGTLTQKR REALERTEKL LETVEQLFLE YAKRSAPFNN WMEGAMEDLQ
     DMFIVHTIEE VQTLITAHEQ FKATLPEADA ERQAILGIQQ EVQKIFNSYG IRGNFTNPYS
     TISTEEIMSK WDKVKKLVPQ RDGALQEELA RQHANERLRH QFAVQANIIG PWIQTRVEEI
     GRCSLELGGT LEDQMTQLKQ CEHLIVNYKP NIDKLEGDHQ LIQESLIFDN KHTSYTMEHI
     RVGWELLLTT IARTINEIET QILTRDAKGI SQEQMSEFRS SFKHFDRKKN GAMDTDDFRA
     CLISMGYDLG EVEFARIMLL VDPNATGVVT FQSFIDFMTR ETGDTDTADQ VVASFRILAA
     DKPYILIDEL RRELPHDQAE YCISRMPPYT GPGAVPGALD YTAFSTALYG ESDL
//