ID   A0A1S3HNG4_LINUN        Unreviewed;       892 AA.
AC   A0A1S3HNG4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Alpha-actinin, sarcomeric isoform X4 {ECO:0000313|RefSeq:XP_013386579.1};
GN   Name=LOC106156043 {ECO:0000313|RefSeq:XP_013386579.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013386579.1};
RN   [1] {ECO:0000313|RefSeq:XP_013386579.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013386579.1};
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   RefSeq; XP_013386579.1; XM_013531125.1.
DR   AlphaFoldDB; A0A1S3HNG4; -.
DR   EnsemblMetazoa; XM_013531125.1; XP_013386579.1; LOC106156043.
DR   GeneID; 106156043; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000085678; Unplaced.
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; 3.
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:SF442; ALPHA-ACTININ, SARCOMERIC-RELATED; 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; 4.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          32..136
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          145..251
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          746..781
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          787..822
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   COILED          266..293
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   892 AA;  103691 MW;  ED2A5C9A6AF2602B CRC64;
     MGDVYQDPYS DGYMEQEEEW EREGLLDPAW EKQQRKTFTA WCNSHLRKVG TQIENIEEDF
     RNGLKLMLLL EVISGEQLPK PDRGKMRFHK IANVNKALDF IESKGVRLVN IGAEEIVDGN
     LKMTLGMIWT IILRFAIQDI SVEELTAKEG LLLWCQRKTA PYKNVNVQNF HLSFKDGLAF
     CALIHRHRPE LLDYDTLSKD NPLDNLNLAF DVAEKHLDIP KMLDAEDMVN SAKPDERSVM
     AYVSSYYHAF SGAQQAETAA NRICKVLKVN QENERLMEEY ERMASDLLEW IRRTTPWLEN
     RHTDNTLPGT QKKLEEFRDY RRKYKPPKLE EKARLETTFN TLQTRLRLSN RPAYLPTEGK
     MVSDIANAWK GLEGAEKGFE EWLLSELQRL ERLDHLAQKF KHKCDIHEEW AFGKEDMLQS
     QDFKKCRLNE LKAMKKKHEA FESDLAAHQD RVEQIAAIAS ELNTLDYHDS PSVNARCQRI
     CDQWDALGTL TQRRRSALEE AERILERIDT LHLEFAKRAA PFNNWMDGAK EDLVDMFIVH
     TTEEIQGLID AHEQFKQTLG EADKEFNSII GLVTEVTRMC QQYDLVLPEN PYTTLSAKDI
     ASKWEEVKLL VPQRDQTLHQ EMLRQRNNDR LRNQFANKAN VVGPWIEKHL DAVASVGMNT
     KESLEQQMQR LKSYEENVLA FRPNMDELER YNQEVQEAMI FDNRFTQYTM ETLRVGWEQL
     VTSIARNINE VENQIMTRDS KGISQEQMEE FRKSFNHFDK NRTRSLEGKE FKACLISLGY
     NIRDDRQGEA DFQRIMSIVD PNGTGRVTFD AFLDFMTRET TDTDTAEQVM QSFKILAGDK
     PYITAEILRT ELPPDQAEYC IQRMAPYSGV DSTKGALDYT SFSTALYGES DL
//