ID G3NZL6_GASAC Unreviewed; 1417 AA.
AC G3NZL6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=CAP-GLY domain containing linker protein 1a {ECO:0000313|Ensembl:ENSGACP00000010789.1};
GN Name=CLIP1 {ECO:0000313|Ensembl:ENSGACP00000010789.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000010789.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000010789.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000010789.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 69293.ENSGACP00000010789; -.
DR Ensembl; ENSGACT00000010811.1; ENSGACP00000010789.1; ENSGACG00000008142.1.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155122; -.
DR InParanoid; G3NZL6; -.
DR OMA; EGKGHNQ; -.
DR TreeFam; TF326096; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000008142; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
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 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:UP000007635}.
FT DOMAIN 79..121
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 236..278
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..379
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 415..491
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1240..1330
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 126..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1417 AA; 156575 MW; 39D86E66E9720D3F CRC64;
MSTAKPSGIK GPSKIGRPPG TGAPKTNPGT GAAGAKVNAV DKSDARVGGG DAESAGGSFQ
VGDRVWVNGN KPGHIRFLGD AQFAPGQWAG IVLDEPIGKN DGSVAGVRYF QCEALRGIFT
RPSKLSLTEG EANGTQTAPP SRAASPTPSV GSVSSQTPAT KSTLPSTTTA TKKASSATPA
APAAPAAPSS NLARTNSESV SNLSETGSVK KGERELKMGD RVLVGGTKAG VVRFLGETDF
AKGEWCGVEL DEPLGKNDGA VAGTRYFQCQ PKYGLFAPVH KVTRIGFPST TPAKAKTTVR
KAAATPSGLK RSPSASSIST MSSVASSVSA KPSRTGLLTE TSSRYNRKIS GTTALQEALK
EKQQHIEQLM AERDMERAEV AKATGHVGEM EQEIGLLRDE QEQDYLFFLK METKMDQLRA
LVEAADKDKV DLLNQLEEER RKVEDLQFRV EEACITKGDL ETQTRLEHAH IKELEQSLLF
EKTKAEKLQR ELEDNRVATV SERSRIMDLE KDLSLRSREV ADLQLRLGTQ QGSEDSNSLS
PLLEEITSLR DQLASQEVKQ QEELTKHREK MEAQEKTHSE TAAQLRATSV SLSGDNEQLQ
MRISQAEKEN ADIIESWRSK LDSVVASHQQ AMEGLKGSFS NGADAQTKEL IETKTELERL
KIEHKLAVEE AAAKHEAHAA AVTREAQALK AQLSSLIEEK ERLEESLRSS VEKAEEQHLV
EMEEVLGKLH NAEVKLNELE EKEAVLTQQA QDKESETKEQ ISEMAALRSQ VAQGNQELVS
LKSQLEAVQS QGNNQGAQVD ALSSQLEGRQ QEVLSLQQSL TTVQQEKEAL EQELGGLKQN
LSEKTEEQTI SSNTMQETLE KLSKKDEQCT SLSTESESLR SQLSGLERKL KASDEKLEQL
SKDKCKLEND ISDMMKTSGD SSVQLTKMND DLKQKERRLE ELQSQLSEEK EKVAHSTEQL
QQEKSRKAQE LMETRDAHQS QISGLQETIA NLEKTVKQGE TLVVELKASQ EKSISQVSEL
HVKEVEVLQS QVNKLKQGLS SSEEKNLELE KLVSELQQYK EQAQATEASG NTAETLEQLT
KEKNKAQSSL EELLSSKQKG EAQLKTLKNN VSKYQEDMNV CKEQLCIETQ RTESLCHEIE
ELKVAVSAKT QSMQMLQDEN NKLTLDVDNN QKALRDLEKL KDEHSKLKKQ LKLSEEQFDK
EKTVFQQSIH KNSALISEKD QQVESLRSEL VGLRGDSDSV KTLQGTIQAL ERDRANLQER
VQRLEKDLPA GSDAINKASG KNDAVSDQLK EAREASESQI EFLNSVIVDL QRKNEELKDK
LEKMVDAALN GNNPSELDNY DSHDKEPLKK KLPPRLFCDI CDCFDLHDTE DCPTQMQMPD
SPPHTTYHGS KGEERPYCDI CEVFGHPTES CNDDQTF
//
