ID A0A1S3P818_SALSA Unreviewed; 2133 AA.
AC A0A1S3P818;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5-like isoform X1 {ECO:0000313|RefSeq:XP_014023745.1, ECO:0000313|RefSeq:XP_014023746.1};
GN Name=LOC106583729 {ECO:0000313|RefSeq:XP_014023745.1,
GN ECO:0000313|RefSeq:XP_014023746.1};
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_014023745.1};
RN [1] {ECO:0000313|RefSeq:XP_014023745.1, ECO:0000313|RefSeq:XP_014023746.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014023745.1,
RC ECO:0000313|RefSeq:XP_014023746.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_014023745.1; XM_014168270.1.
DR RefSeq; XP_014023746.1; XM_014168271.1.
DR GeneID; 106583729; -.
DR KEGG; sasa:106583729; -.
DR CTD; 567481; -.
DR OrthoDB; 5489926at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.58.60; -; 13.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.920.20; Gas2-like domain; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; ENVOPLAKIN; 1.
DR PANTHER; PTHR23169:SF34; MICROTUBULE-ACTIN CROSS-LINKING FACTOR 1, ISOFORMS 1_2_3_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00435; Spectrin; 6.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00150; SPEC; 13.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF143575; GAS2 domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 12.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51460; GAR; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 1885..1920
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1921..1956
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1961..2033
FT /note="GAR"
FT /evidence="ECO:0000259|PROSITE:PS51460"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2109..2133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2133 AA; 243316 MW; B8C153399044B811 CRC64;
MGNLISRPSC LGQKSKQVRS DEDFLKECYQ RRREWQAPPL THHGEARREE VVREREEEEE
RVTDRTKEDE VEDEVSHSNT PPSDKPLRTN TSPAPTVTTT STLDNAWHGT PSPIKTSRNS
TLTRKAVVQE IPYGRSPLAL PGSVPGSAER RASLQRKDSR EGSLQRRDSR EGSPWSWKTL
ASREVTEVTE VTETVVTEIV EVTEYPSGEK GGDPIVTRTV RVLTGAAEEL AELQSDGHSS
SDQDSSLDRW RGTRSALTLR DDFADSETFH QSLEALLTWV CEIEELTANQ KPPSSEVKVV
KAQLQEQKLL QRLLEDRRHS METMMLEGPH MAEAFPGEEG EQARVQLSTL RHKWETLLVD
AVNRRGNLEL ILPRAKLFQE RVDSLQQWLI SVEQDLAKLR NFEREMLHLP EGTEEAKAVV
EEIKGKNADL VKIQQSGHDL KEKISEEEAQ QVQERVDSLR IRCSVLSLTS GDVLQRLEQA
LEASSRCTSS QEDLHLWLGR IERDLLGPAG GQTGGGDTVL CAAERQRLEQ AVVKEMAWFR
DTALGLEQLK AFTLEPELIS AQLYEQKILA VEILQHKFNI EKMVKIAEIL QTYGDEGEIR
DLQTPLDALQ EQCNTTSATN SHVVLQLEHA QSLLVQFTEG FAEVSPWLQE TQALIGQLSL
STISYKAFRE QQDLLQGLRE SIAEHRPLIA RLCSLGKRLS ELSPAQGEEF CHSATEAEEQ
HRAIRDRVRE AANLLEESLP RYTQLNERMT LIRESLDRLL GHMQSPVSLQ GHTPRIQEQL
QDNKHTLAEL SKLELGLGSV RTQADELLAN TLAAGDASIG TAIQEQVSSL TQLWEEAQKQ
AQERDGWLLN LLDLALKFWN DVSDVTAGLN DAQQAVLDLN ASRTDSETIR QSLETMQTLR
KDIDSLQGEL DTLGILGMDL MSACGDTDKP DVTKSLDELY CTWNNLSKLW SECHKKLEES
LQMALHYQDT IQGLFEWLKS AELRSTEEFL VGTDLESVKE QLCDLKEFKR ELYQKKIEME
SLNHRFVCRL SPGSERPGSV SPLCDFRQRW DSLEAETVSR QHQLECALLG LGQFQNTLDE
LHTWLSHTAD LLQCSRPISI DLQACEIELA KHKVLRNDVM SHVRTVESLN QAGRGLLEVG
TGDSPHGLHP RLEQLNERWE FVRCETERRQ LQLENNLSQV QDVTMEIQDL LQWLENTDLR
LSSSKTVWGM PDSASERLNA HLELCNEMDS KLHAYTDVRN AIRRMLESSD VTRGSSTEHS
LCILEQKWAT VYGKVQDRKA KLTEGLSLAK EFHCNVQELL TRMAKCEEAI GVLPVPSFVL
DTVCGQLQDH RTLVSEVNCY GEKKTVVESA GSRLTELSRK EDCDVVHNLI MTVHDRYRKL
HQRATERGRT LEDVKKNAKQ FSESWRLLVD WMTEVEQTLD THKEIAVDHE EIKLQLTEQK
DFQKLLRSKR PMYEATLKSG RGLHERSQSA QDRQHLENLL SELRDSWDTI SGKSMERQHK
LEEALLFSGR FTDALQALND WLYRAEPQLA EDVPVGGEKD MVNNLIDKHK VFQKELGKRA
GCIRTLKRSV RDLTRSSTAD AHWLQEQMDE LEARWEDVCK LSVSKQARLE AALQQAEKFD
RLVHSFLEHL AEAERVLRYG VIPEEEEALL AFRKQHEKSI TSLRSQEMEL ESIRCLNEEI
LSSCHPDSII TLKSWISVTK TRYEEVQTWA QQQGQRIQAS LSALEVEREK LQRLLDWISS
AEEALNLRDQ EPPAESIEHN QELIVQHMVF MEELNQKLPE VEHATKSCKQ KLIPKQQASP
CRKALTKRRS TLKLQPTVVP LPLENLDPQT PQLCQLVSHW QKLWLLALAR QGRLEQHEQG
LQEMEEFANF DFNVWRKRYM QWISHLKSRI LDVFRNIDRD QDGRISKKEL IDNVLASKFP
TNSLEMNAVA NIFDMNGDGF IDYYEFVSAL HPSRDPYRRT LDADQINEEV GRQVSQCNCP
KRFQVEQISA NRYRFGDSQQ LRMVRILRST LMVRVGGGWT ALDEFLVKND PCRVKGRTNL
KIKEKYLFDN SRRGGSSKTL TVSRSNSSLS LYSSASAPSS PLTRKALLRR SLSGDRCIRP
RSSIAALGSD LQFSTAGDDD SLSPSEEAER LPT
//
