ID A0A1S3MV49_SALSA Unreviewed; 1556 AA.
AC A0A1S3MV49;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=CLIP-associating protein 1-B-like isoform X8 {ECO:0000313|RefSeq:XP_014006980.1};
GN Name=LOC106575187 {ECO:0000313|RefSeq:XP_014006980.1};
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_014006980.1};
RN [1] {ECO:0000313|RefSeq:XP_014006980.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014006980.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Golgi
CC apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
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DR RefSeq; XP_014006980.1; XM_014151505.1.
DR GeneID; 106575187; -.
DR OrthoDB; 5478662at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
DR GO; GO:1902903; P:regulation of supramolecular fiber organization; IEA:UniProt.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR21567; CLASP; 1.
DR PANTHER; PTHR21567:SF28; CLIP-ASSOCIATING PROTEIN 1; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 4: Predicted;
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..232
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 168..206
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 315..548
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1312..1546
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 234..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1556 AA; 171594 MW; F47D6868EF148C0B CRC64;
MEWNMEYCME QVMQKDLGRR LQVGQDIIDS ILDKDKSQDL EQDQTMLDRM VDGVATNWVN
SSNFKVALLG MDILTALVTR LQERFKTQIG TVLPSLIDRL GDSKDQVRDQ DQALLLKIMD
QAANPQYVWD RMLGGFKHKN NRTRESVCIC LIATLNVYGA QGLTLSKIVP HICNLLGDPT
SQVRDGAMNC LVEIYRHVGE RVRMDLGKKG LPQSRLNVIF SKFDEVQRSG NMILSPVSDK
NYDDDDSVDG GRSSSSKGPT SGKKAVSMGS FRRPGSASST KSTGRDGPSA AAAGAVDEED
FIRAFEEVST MELFSNREME DAMTKIREVL ADDKRDWEHR VTALKKMRSL LLAGAVEFDG
FSQQLRLTEA AFKMSAKDLR SQVVREACIT LGHLSFVLGN RFDHCAESIM PTLLTLVSNS
AKVMATSGIA VIRLIIRHTH YPRLIPIVTS SCQSKSVAVR RRCFEFLDLL LQEWQTNSLE
RNVAVLTETI RKGVHDADSE ARSVARKCYW TFHGHFSREA EQLFQALESS YQKALQSHMK
SSDSILSLPA SDRSSSSSQE SLNRPQSAKS SVGNTVTRTK AAPARGPSTP RSLQRSRSDV
DVNAAATASA KSRMTPVPGS PAPFSAASAL PPGSYASLDN TPGNIRPVGR VRTRRTSAGS
GVGASPSVID SRGRSRAKMV SVSQPGSRSG SPGRLLSHTY GRISRATGGT TPAESRPKVP
RSHGCSRDTS PDRSGLERLG LAHQARISAS VNAMRILNTG TEVEAAVADA LLLGDARNNK
RRPVRRRYES PGIYSDDDAN SDASSACSER SYGSRNGGPP HYMRQTEDVA EVLNHCASSN
WSERKEGLLG LQNLLVSQRI LSRVELKRLC EIFTRMFADP HSKRVFSMFL ETLVDFITLH
REDVQDWLFV LLTQLLKKMG ADLLGSVQAK VQKALDVTRD SFPFDQQFNI LMRFIVDQTQ
TPNLKVKVAI LRYIECLARQ MDPADFVNSS ETRLAVSRII TWTTEPKSSD VRKSFHHSWA
GEELSGRPSI TIASLPGEGN VEERCKQAAQ VVLIALFELN TPEFTMLLGA LPKTFQDGAT
KLLHSHLRNS SSTGVASPSN TMGRTPPPPR HPSSRSSPLT SPTNCSHGGL SPSRLWGWSA
DGLSKYPPPF PSPLSSTPAA PSLKTLRSAY SPSMLEYDTE NLNTDEIYSS LRGVTEAIQN
FSFRSQEDLM EPGRGKREDT PGVGTASHSG VDVVEGPGGR TALDNKTSLL NTPSPRSFSG
PRGRDYNPNN YSDTISAYDK AALRETVYED DVEQLRDGRQ ECGGENKMLR TKNSSPAEQL
ELVGELLKEL SNPSERPEER RGALVELLKI AREDSLAVWE EHFKTMLLLL LETLSDQDNT
IRALALRVLK EILRNQPARF KNYAELTIMK TLELHKDSHK EVVRAAEESA STLAGSIHPE
QCIKVLCPIV QTADYPINLA SIKMQTKVIE RITKESLHQL LPDIIPGLLQ GYDNTESSVR
KASVFCLVAV YSVIGEELKP YLAQLTGSKM KLLNLYIKRA QTSTSNSSSS SDISSY
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