ID A0A3P9A7H8_ESOLU Unreviewed; 2215 AA.
AC A0A3P9A7H8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=CAP-Gly domain containing linker protein 1 {ECO:0000313|Ensembl:ENSELUP00000036588.2};
GN Name=CLIP1 {ECO:0000313|Ensembl:ENSELUP00000036588.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000036588.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000036588.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000036588.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 8010.ENSELUP00000036588; -.
DR Ensembl; ENSELUT00000025336.2; ENSELUP00000036588.2; ENSELUG00000015932.2.
DR GeneTree; ENSGT00940000155122; -.
DR InParanoid; A0A3P9A7H8; -.
DR OMA; DAENRCS; -.
DR Proteomes; UP000265140; LG13.
DR Bgee; ENSELUG00000015932; Expressed in heart and 15 other cell types or tissues.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
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 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:UP000265140}.
FT DOMAIN 76..118
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 219..261
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2068..2088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 342..467
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 523..800
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1048..1078
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1135..1334
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1370..1572
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1637..1727
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1868..1916
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1999..2067
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2098..2125
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 124..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2215 AA; 247704 MW; 0687CF716C3B4B2E CRC64;
MSTAKPSGLK APSKIGKPTG ASATKTTLFA GQKVAAADKS APVDSAAGAQ DVGQNFQVGE
RVWVNGNKPG VVQFLGEAQF APGQWAGIVL DEPIGKNDGS VAGVRYFQCE PLKGIFTRPS
KLSYTEGEAS GTQTAPQSRA GSPTPSTASV ASHTPSVKKA PATTPATPAT PASNLARTNS
ESVSNLSDTG SVKKAERELK SGDRVLVGGT KAGVVRFLGE TDFAKGEWCG VELDEPLGKN
DGAVAGTRYF QCQPKYGLFA PVHKVTRIGF PSTTPAKAKT TVRKAGATPT GLKRSPSASS
ISSMSSVASS VSAKPSRTGL LTETSSRYSR KISGTTAVQE VLKEKQQHIE QLMAERDMER
AEVAKATTHV GEVEQELTLL REDQEQMEAK MDQLRTLVEA ADKEKVELLN LLEEEKRKVE
DLQFRVEEAC ITKGDLETQT KLEHAHIKEL EQSLLFEKTK AEKLQRDLED TRVATVSEKS
RIMELERDLV LRTREVADLR LRLETQHGSQ GSDSITSPLL EEVSSLRAQL ASQEDQYRAE
LTEMKEKMAA EEKAHNEALA QLHVSSTKIS TDNEQLKLRL SQNEKENAEV IELWRSKLES
AIASHQQAME ELKVSFSQGA SSQATELVET KSALERLKAV HMQALEETEA RFKAESAARA
RETGELNKQL LVLLEEKERL EESLRSSVES AEEQHLVEME DVLGKLYSVE QKVKEQEAKL
VQQSQERAKE VREQAEAMEA LRIQSGQGNE VLESLRTQLK EAERQACSQG SKVSELISEL
EGKQQELLSL QKSLTSVKQD KGSLEQELGV VKNQLSERAD DHTKSTQTIQ ELLQKLGQKE
EQCTLISSES EALRSQLAGM ERKLKAGEEK LEQLTSDKAK LQSDISDMMK SSGDSSAQLT
KMNEDLTKKE RLFEELQTQL AIEKDRAAYS EEQLQQEVAR KERDRKSAEE EHQGQLRKLQ
EKITQLEKSL QQGEAQALLL QTSQQKALSE ASEHHARQLQ ELQSLADKSM HELSVSKDKA
QELERLVAEL QPFKDKFQFL SAELDSSKQH VERLSTDLEK QISELENKSK ESLDLQAQRG
MLEKQLLEHQ AKLSASEASH NDLSGKIEEL TTLRDKLKKG QEDLLMTNSQ LDGEKACLSR
ELAKLRVALE EAQVANKGLS QSEADHQSQI EELQRKNAEK HDFLLKLEQE IQQQETKRKQ
LADVYEKTCE ERNKLQEELK QSCEKLISEK NTLLCERDAA RNAKKSLDAR NVELKARCQS
LSLEKEDLCV KNAQLQAQTE TLGNDKVNMF AQMNATISDK EALQALNADL QIQLNNTQKN
LEKSVRDNNE LNASKLSLVK MLEESKTTTE VTDSERLQLM QEKEDLLAAQ RKVCSEKDEL
LKEMKELKEK LRLSIEEVAT SKEKVTEMFT SYSKEKEAVC LQNAETEKLL NSLRKEKIAI
ESTLEQQKME CDCLVHQNEE LEEKHTKEVL EKVSLTKMCN KLAGEIQDMK EQLEISSKAI
DDLKQANSHL TSLLEESAQN IQKLEVEGVS LKKEKADLLV QLQQHVSENE VLEKSQIELS
EENHKLKGIS DQMCLELTQQ SDTLRKECDV LLSHQEELNK SIASACGERD KMITERNSLH
CQLEELKTTH TSLLGERNCL LEENAQMQAI VQDLTQKSVT GDKAIDELSA ILKDIGEERK
SLAQEVENLK TLLKQEVLEK DSLVEDRKQM SAKLEDLGKE VSSMAKEKVD RLAMQSKLEQ
NLCSLHSSQE SSNVEHSRLL EEVTNLKAIQ TQLEANVQAL HAEKTVIEGQ HKVSVEEALA
SAKAREEIVT TLEDLKVQKD AMISERDRST QQVTHLENQL KTTLCQQLEA AESSAKTAEA
MGQLIKEKDR LLQEKSDTQS LLDELRSSKQ EITNQLDALK QQNFKLQEEL KLSREQRSLG
NQKISSLSQE IEELKSTALL KSQSLVAIQQ ENTKLTNELS SRESTDQQKL EAQQSILNKQ
LQEIKHSLPN NTYRETILKN QLEEEKASLQ KCVHKSSDKD QELETLKSEL SVLRAESATA
MTLKSTVQSL EKDKARLQQL VQNLEKSLAG GKDAVSGSSD ATACDQGREE KVTAESQIDF
LNSVIVDLQK KNEDLKGKLE KMAEAALNGN NASELDTYDS SLKGPSKKKV PPRLFCDICD
CFDLHDTEDC PTQMQMPDSP PHTAYHGSKD EERAYCDICE AFGHWTDNCN DDQTF
//
