ID A0A1S3Q0N6_SALSA Unreviewed; 1485 AA.
AC A0A1S3Q0N6;
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 2 isoform X29 {ECO:0000313|RefSeq:XP_014033528.1};
GN Name=clasp2 {ECO:0000313|RefSeq:XP_014033528.1};
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_014033528.1};
RN [1] {ECO:0000313|RefSeq:XP_014033528.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014033528.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000256|ARBA:ARBA00004629}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|ARBA:ARBA00004601}.
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DR RefSeq; XP_014033528.1; XM_014178053.1.
DR OrthoDB; 5478662at2759; -.
DR Proteomes; UP000087266; Chromosome ssa27.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:SF30; CLIP-ASSOCIATING PROTEIN 2; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 8..233
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REPEAT 169..207
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 314..547
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1234..1481
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 262..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1250..1284
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 541..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 163611 MW; C5E7B924A5854853 CRC64;
MEEHDNMDYF YQQVLQKDVT RRLQVGQDLI DYLNDPQRSS DVEQDKPRLD KTVDELTGWV
NSSNYKVALL GIDIAGAFVD RLGERFRGYL GTVVPALVDR LGDSKDQVRE QSQTVILRCM
EVTASPMYVW ERLLPGFKHK NFRSREGVCL VLCATLNTYG AQPLSLSKIV PYLCSLTGDQ
NPQVREAATA SLVDVYRHIG ERVRADLGKR GLPATRLQTI YGRFDEALNS GNMALSPSHD
HSFEDDVDST DGNRAQAAFK VPKIPKKPAE SSTARRPSAT GPKIGGASKD GAGGIDEEDF
IKAFTDVPTV QIYSSRDLED NLNKIREICS DDKHDWDQRA AAMKKIRSLI VAGATEYECF
FQHLRLLDGA FKLSAKDLRS QVVREACITV AHLSTVLGNK FDHGAEGILP VLFNLIPNCA
KVMATSGVSA IRFIIRHTHV PRLIPLITSN CTCKSVAVRR KCFDFLDLLL QEWQTQTLER
HTAVMVASIK KGIADADAEA RVEARKAYWG LRNHFPGEAD TLFNSLEPSY QRSLQSSLRN
AGSVASLPQS DRSSSSSQES LNRPLSSKWS AVPGRDDASD KMDGRLRTKQ PLTTATSVSQ
VDSRGRTRTK MVSQSQRSQS ATPIGAGSRS GSPGRVLTST ALSTLGSGAQ RVLAGTGGRR
SRIPRSQGCS RDSSPTRLSV APSSISSIYN GASRGARGSR IPRPSMSQGC SREASRESSR
DTSPARSFTP LASRHYSRST GALHTADALG AAGSGYSISQ SSRLSSSVSA MRILNTGSDV
EEALADALLL GDMRSKKKPA RRRYENYGMY SDDDANSDAS SACSERSYSS RNGGAIPTYM
RQTEDVAEVL NRCASANWSE RKEGLLGLQA LLKNQRTLSR VELKRLCEIF TRMFADPHSK
RESGSRVYGT AESGISSASF KRVFSMFLET LVDFVLVHRE DLQDWLFVLL TQLLKKMGAD
LLGSVQAKVQ RALDITRESF PNDLQFTILM RFTVDQTQTP NLKVKVAVLK YIETLTLQME
PQDFVNSSET RLAVSRIITW TTEPKSSDVR KAAQSVLISL FQLNTPEFTM LLAALPKTFQ
DGATKLLQNH LRNTGNAAQA PTGSPLTRHT PRSPASWSSP LTSPTNTSQN TSSPSAFDYD
TENMNSEDIY SSLRGVTEAI QNFSVRSQED MNEPVRRREG EEGGSAGADQ VDGGRTALDN
KTSLLNTPLL SSSPRGSRDP FTDSPFKHSV IDTSLDESDQ QTDDSSIDQS ELVSELLKEL
SNHNERVEER KAALCELLKL IRENTLQVSW DEHFKTILLL LLETLGDREH VIRALALRVL
REILSRQPWR FKNYAELTIM KALEAHKDPH KEVVRAAEET AAMLASSISP DQCIKVLCPI
IQSADYPINL AAIKMQTKVI ERVPHEGLVS MLPEIVPGLI QGYDNSESSV RKACVFCLVA
LYAVIGEELK PHLNQLSGSK LKLLNLYIKR AQSGSSGGEP PADSL
//
