ID A0A1S3SR00_SALSA Unreviewed; 1325 AA.
AC A0A1S3SR00;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Calmin-like isoform X1 {ECO:0000313|RefSeq:XP_014066773.1};
GN Name=LOC106611269 {ECO:0000313|RefSeq:XP_014066773.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014066773.1};
RN [1] {ECO:0000313|RefSeq:XP_014066773.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014066773.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014066773.1; XM_014211298.1.
DR GeneID; 106611269; -.
DR KEGG; sasa:106611269; -.
DR OrthoDB; 5478539at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR CDD; cd21245; CH_CLMN_rpt2; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR047826; CLMN_CH_second.
DR PANTHER; PTHR47535:SF9; CALMIN-LIKE; 1.
DR PANTHER; PTHR47535; MUSCLE-SPECIFIC PROTEIN 300 KDA, ISOFORM G; 1.
DR Pfam; PF00307; CH; 2.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1292..1311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..142
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 191..295
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 154..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 146808 MW; EC970D028C1D6FD3 CRC64;
MAGHEWEYKD WFEREEFIGQ ISDIRVQNLQ VEREVVQKRT FTRWMNLHLE KCTPPMEVND
LFRDIQDGRI LMALLEELSG CKLLHGWKPS SHRIFRLNNI AKVLTFLEER NVKLVSIDAA
DVADGNSSIV LGLIWNIILF FQIKELTGNI KSQFPSSSSL SSLPTSSDSD TSHSSTPSFE
RPRSIAMRDH GKPIKTLLQW VQRRTRKYGV AVQDFGKSWT SGLAFLAVIK SIDPSLVDMR
RALLRTAREN LEDAFRTAHY SLGIPRLLDP EDVTINPPDE QSIMTYVSQF LEHFPGMEEL
QENASDVIQR SVSSGRLSCR VNDSSHDLMN GVHRSRDRER PYVVRRDWVQ PPPKILISSV
SEELKSPTSP VAVERSWVNE GSSVGSTSSP VFTVSTSSSP QPSFVDSVIG SVSCDSPISD
SVIGSPDSCW EGHPNEAVTP DRFVESRSDG SLCDSGLSWD MNIPPSTPHG VTPDLEEPLP
SVTGLTGKPQ DEEQEVIPEL FVDEGNYSLN SLVSTQDRSR THPEKEEDGG EREEDGGERE
EDGGRKEEEE YNYILNLSVD KAGKQEPDQR EGNNKYRSST GQSNSVNKEQ GWPSLELSDE
PQETDSDQKG ESVCGGESVC GGERGGAVSS PQHEKISQSK QGSDITHQVT PDLHEEPNQR
DSVPETTDRT SECAKKETAE PSRDSRKAGN PEEELAKERS DKAEGQSDVT DRVEMEHRQT
TSLSERDRDG ERSLEGSEER HKQVTEESET QEKITDVQNG HVESQENTTT QVDDVTESTH
PQPYMEMDQS RTILGGPSEQ CLDPVEQSHT GTTPACTDGG QSSTLLTEAG KEGTLSPEIE
AEAGDEDLCG PPGGGLVERT GKCERASCVG DADVNVVAPE EKRVAEKEHD WVDGSGTTDN
TETVVEVPHQ CKPVSIIPLD MVYYPHYDVH ISQVIEAFVE PNPGSVLTGL VPQSPLSDTN
TQSQAVLHSQ EERDSEKDTG DHTDGGHSET EASAVEETGD KMADTEQSET KPVNMTYTDT
ERRSALGSES EPMDLFHTDS DANESSRSAL DEPMTVSDTL EPMDLFYPDT DDCGPVEEPE
NDVETSPWSS SFSKSVETWP STFSVAALKP APSSEPEPLP ETHTQTHTDS HTHNTLYQEE
LCEVSTTQEH DKAPLSQHHP HYQEIEVRGG SGGSDLQERC SMLGEQTAGD GTVVETHRGP
AESSDLTMTD EERPGSAAAA ARESNETVRR NADSDGILDD QCSMCFTPLH KRKNNGSNEK
DNQKGLASSR THCTKSDTSW REMWIPTSLT EYYIILLLWL VLYCLLVLPQ IHYRDLPRLL
LNLDE
//
