ID A0A1S3PGU5_SALSA Unreviewed; 2279 AA.
AC A0A1S3PGU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=CAP-Gly domain-containing linker protein 1-like isoform X12 {ECO:0000313|RefSeq:XP_014026826.1};
GN Name=LOC106585282 {ECO:0000313|RefSeq:XP_014026826.1};
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_014026826.1};
RN [1] {ECO:0000313|RefSeq:XP_014026826.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026826.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014026826.1; XM_014171351.1.
DR STRING; 8030.ENSSSAP00000103369; -.
DR PaxDb; 8030-ENSSSAP00000103369; -.
DR GeneID; 106585282; -.
DR OrthoDB; 2914056at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR PANTHER; PTHR18916:SF44; CAP-GLY DOMAIN-CONTAINING LINKER PROTEIN 1; 1.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 2.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 77..119
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 217..259
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 340..465
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 490..524
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 590..731
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1702..1771
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2161..2191
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2279 AA; 255056 MW; E4FDF6326A0779EA CRC64;
MSQAKPSGLK APSKIGRPTG APATKTSPST AGSKVVAADK STPGGGAVGT QDGGENFQVG
ERVWVNGNKP GVVQFLGDAQ FAPGQWAGIV LDEPIGKNDG SVAGVRYFQC EPLKGIFTRP
SKLSYTEGEA NGTQTAPPSR AGSPTPSTAS LASHTPSVKK ASTAMPATPA SNLARTNSES
ISNLSDTGSV KKGERELKNG DRVLVGGTKA GVVRFLGETD FAKGEWCGVE LDEPLGKNDG
AVAGTRYFQC QPKYGLFAPV HKVTRIGFPS TTPAKAKTTV RKVVATPSGL KRSPSTSSIS
SMSSVTSSVS AKPSRTGLLT ETSSRYSRKI SGTTAVQEVL KEKQQHIEQL MAERDMERAE
VAKATTHVGE VEQELTLLRD DQEQMEAKMD QLRTLVEAAD KEKVELLNQL EEEKRKVEDL
QFRVEEACIT KGDLEVATVS EKSRIMELER DLVLRTREVD DLRLRLEAQQ ESEGSDSTTS
PLLEEVSSLR AQLASQEDQQ RVELARMREK LAAEEKAHSE AMAQLQVSST KISTDNEQLK
LRVSQNEKEN ADVIELWSSK LESAITSHQQ AMEEMKVSFS KGAGSQVTEL VETKSALERL
KVEHKQALEE AGARCEAEAA ARARETGELN KQLLVMSEEK ERLEESLRSS VESAEEQHLV
EMEDVLVKLH TAELKVKELE EQEAKLVQQT QDRAKEVQEQ VAAMEALRSQ AGQGNQELQS
LRTQLEEAQR QACSQGNKVS ELSSELEGRQ QEILSLQQSL TSVQQNTGSL EQELGNLKQK
LSESTDDQTK STQTMQELLQ KLGEKEEQCT SLSTESEALR SQLAGLERKL KAGEEKLDQV
VNDKAKLQSD ISDMMKSSGD SSAQLTKMNE DLTQKERKLE DLQTQLAEDK EQRAHSEEQQ
QQEVARKEQE HQGQLSNLQE KITQLEKSLL QGEAQAKELQ TSQQKALSQA SEHHAKQLKE
LQTSQQKALS QASEHHAKQL KELQGQVDQT KQELSVSREK AQELERLVAE LQPYKEKAQF
LSAELDSSMQ HVERLSTDLE KQISALEHMS KESSVLRAHK ECLEKQLFEL QAKLSALEAS
HNELSVKTEE LLTLRDTLTK EQEELLTTNQ QLDGEKASLS REIEKLRVAV EEAQAKNESL
SQFEMEHQSQ IEELQKTNAE KQEVLLKYKQ EIQQQETKRN QLAEIYEKTC EERNGLQEEL
KQSREKLISE MDSLVLERDA ARNAKKSLES KNTELQTRCQ SLSLEKVDLC VKNTQLQAQK
ETLARDKEEM SAQINAAISD KEALQAMNTE LQNQLNITKK DLEKSVRDNS ELQASKMSLA
KMLDESKTSS EVTDSERLHL MQEKEDLLAT QRKVCSEKDE LLKEIEEFKE KLRLSTQEAA
TSKEKVKEVL SSFAKEKEAL CLQNEETEKA LHSVRKEKLA MESTLEQQKM ESDRLVHEKE
ELEEKHTKEI SEKATLTKER DKMAGEIRSM KDQLDSSSKA IDDLKQANYN LTSLLEESKQ
KIQKVEVEGA SLKKEKADLQ AQLQKRCSER EALEKSKTEL AEEHHKLKGN SEQVHLELIQ
QRDTLRKERD LLHSQQAELN KNLQILQKDK DDLLLQVQEF KGQTESLSKE KRLLESQQQT
EATERSKLSS AKDDLSRERE DLQSQMSTLT QKNTSLLQTE SILKAEIASV CVERDTMASE
KNSLCCDLKQ LKMTHTGLLG EQHGLLEENA QMQAKVQDLT QKSVTRDKAI DELSASLKDI
GEERKALARE VENLKAQLKQ RDQEKDGLAE DQECLFNKLE ELGKEGSSLA KEKVDLLAIQ
SRLEENLSSL HSSQKSGDEE RSRLLEEVEK LRAAQTQLEA DAQTLRAEKA GLEGQHKVSV
EEASVSAKAR EEIGTKLEVL KVEKDALLKE RDEATQQVTQ LEAQLKNILS KQLEAAESSG
KTAEAVERLT QEKGRLEQEK SEAQSLLEEF RSAKQEMTSQ LDALKQQNSK YQEELNLQLC
SENQKISSLC QEIEELKQVA SVKSQSLVAL QEENNKLTKE VGSSKKETSG QQKLETQQSK
LNKQLQDMKQ RETALKKQLD EEKASLQKSI HKSSALISEK DQELETLKSE FSVLRGESAT
AKTLKSTVQS LEKDKSRLQE RVQSLEKSLA GEQDTLTSAS GDAALHQLKD DKEASESQAA
IEFLNSVIVD LQKKNEDLKG KLEKMAEASL NGNNARELDN YDGGFNEGPS KKKVPPRLFC
DICDCFDLHD TEDCPTQMQM PDSPPHTTYH GSKDEERAYC DICEAFGHWT DSCNDDQTF
//