ID A0A663EA66_AQUCH Unreviewed; 1409 AA.
AC A0A663EA66;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE SubName: Full=CAP-Gly domain containing linker protein 1 {ECO:0000313|Ensembl:ENSACCP00020008846.1};
GN Name=CLIP1 {ECO:0000313|Ensembl:ENSACCP00020008846.1};
OS Aquila chrysaetos chrysaetos.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC Accipitriformes; Accipitridae; Accipitrinae; Aquila.
OX NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020008846.1, ECO:0000313|Proteomes:UP000472275};
RN [1] {ECO:0000313|Ensembl:ENSACCP00020008846.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR Ensembl; ENSACCT00020009231.1; ENSACCP00020008846.1; ENSACCG00020005676.1.
DR GeneTree; ENSGT00940000155122; -.
DR Proteomes; UP000472275; Chromosome 9.
DR GO; GO:0005938; C:cell cortex; IEA:TreeGrafter.
DR GO; GO:0035371; C:microtubule plus-end; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:TreeGrafter.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:TreeGrafter.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:TreeGrafter.
DR FunFam; 2.30.30.190:FF:000002; CAP-Gly domain containing linker protein 1; 1.
DR FunFam; 2.30.30.190:FF:000001; Putative CAP-Gly domain-containing linker protein 1; 1.
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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000472275};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 79..121
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 235..277
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 132..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..378
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 404..452
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 511..1178
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1204..1269
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1295..1344
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..164
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..333
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 157940 MW; 63ED10EA6BA37BA4 CRC64;
MSMLKPSGLK APSKTIKHGS TLLKPPASVA AAPVEKAASS EKASSATTAD AHEEFVDDFR
VGERVWVNGN KPGFIQFLGE TQFAPGQWAG IVLDEPIGKN DGSVAGVRYF QCEPLRGIFT
RPSKLTRKVL TEDEANGTQT AHASRATSPT STSAASMVSS SAAALPPSGI PQKTSPLAAK
EHSTPSQITN LSKTASESIS NLSEAGSLKK GERELKIGDR VLVGGTKAGV VRFLGETDFA
KGEWCGVELD EPLGKNDGAV AGTRYFQCQP KYGLFAPVHK VTKIGFPSTT PAKAKTTVRK
VIATPTALKR SPSASSLSSL SSVASSVSSK PSRTGLLTET SSRYARKISG TTALQEALKE
KQQHIEQLLA ERDLERAEVA KATSHVGEIE QELALVRDGH DRHVLEMEAK MDQLRAMVEA
ADREKVELLN QLEEEKRKVE DLQFRVEEES ITKGDLEVAT VSEKSRIMEL ERDLALRVKE
VAELRGRLES SKHMDDVDTS LSLLQEISSL QERMAAVSKE HQNEINSLKE KFGISEEALQ
KEIKSLSASN ERMAKENESL KTKLDHANKE NSDVIELWKS KLESAIASHQ QAMEELKVSF
SKGVGAQTAE FAELKTQIEK IKLDYENEMS NLKLKQENEK SHHLKEIESL KAKLLAVTEE
KEQNLESLKT KLESVEDQHL VEMEDTLNKL QEAEIKVKEL EVLQAKYNEQ TKVIDSLTPQ
IKAAEEKLLD LAALQKANSE GKLEIQKLSK QLEAAEKQIQ NLETEKVDGS SKASNLAKEL
QGKEQKLLDL EKNLSAVNQV KDSLENELQV LKDKFTSAAD EAENVQQTMQ ETIKKLNQKE
EQFALMSSEL EQLKSSLTVM EKKLKEREER EQQLIEAKAK LENDIAEIMK SSGDSSAQLT
KMNNELRLKE RQLDQIQLEL TKANEKAVQL QKNVEQTTQK AEQSQQETLK IHQAELKNMQ
DQLTDMKKQI ETSQNQYKDL QAKYEKETSE MITKHDADIK GFKQNLLDAE EALQIAQKKN
DELEKQAEEL KNQAEQAKAA KMAEDVFQTV EKVTKEKDAI HKEKIETLAS LENSRQTNEK
LQNELDMLKQ NNLKNEEELN KSKELLNLEN QKVEELRKEF EALKLAAAQK SQQLAALQEE
NVKLAEELGR SRDEVTSHQK LEEERSVLNN QLLEMKKSLP SNSLRESTLK KEIDEERASL
QKSISATSAL ITQKDEELEK LRNEITVLRG ENASAKTLQS VVKSLESDKL KLEEKVKNLE
QKLKENNEQP LTVTSSSDDI AANLLQDEIA KEKQIDFLNS VIVDLQRRNE ELNLKIQRMC
EAALNGNEEE INNYDSEEES LSKKKPRLFC DICGCFDLHD TEDCPTQAQM LEEPPHSAYH
GSRREERPYC DTCEMFGHWT ADCNDDETF
//
