ID A0A4W2E1D7_BOBOX Unreviewed; 1427 AA.
AC A0A4W2E1D7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=CAP-Gly domain-containing protein {ECO:0000259|PROSITE:PS50245};
GN Name=CLIP1 {ECO:0000313|Ensembl:ENSBIXP00000032656.1};
OS Bos indicus x Bos taurus (Hybrid cattle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000032656.1, ECO:0000313|Proteomes:UP000314981};
RN [1] {ECO:0000313|Ensembl:ENSBIXP00000032656.1, ECO:0000313|Proteomes:UP000314981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT "Haplotype-resolved cattle genomes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBIXP00000032656.1}
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; ENSBIXT00000018035.1; ENSBIXP00000032656.1; ENSBIXG00000002183.1.
DR Proteomes; UP000314981; Chromosome 17.
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 Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
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:UP000314981};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 78..120
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 232..274
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 152..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..377
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 302..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 160695 MW; 9DDCAAD941347DE2 CRC64;
MSMLKPSGLK APTKILKPGS TALKTPAAVA SPIEKTISSE KASSTLSSET QEEFVDDFRV
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CELLKGIFTR
PSKLTRKVQA EDEADGPQTP HASRATLSLS TSGISMASSS PATPSNIPHK SSQPTAKEPS
ATSQISNLTK TASESISNLS EAGSIKKGER ELKIGDRVLV GGTKAGVVRF LGETDFAKGE
WCGVELDEPL GKNDGAVAGT RYFQCQPKYG LFAPVHKVTK IGFPSTTPAK AKAAAVRRVM
ATTPASMKRS PSASSLSSMS SVASSVSSKP SRTGLLTETS SRYARKISGT TALQEALKEK
QQHIEQLLAE RDLERAEVAK ATSHVGEIEQ ELALARDGHD QHVLELEAKM DQLRTMVEAA
DREKVELLNQ LEEEKRKVED LQFRVEEESI TKGDLETQTK LEHARIKELE QSLLFEKTKA
DKLQRELEDT RVATVSEKSR IMELEKDLAL RVQEVAELRR RLESNKPAGD VDMSLSLLQE
ISALQEKLEA THSDHQKEVA SLKEHFGARE EMHQKELKVL QAATEKLSKE NESLKSKLDH
ANKENSDVIA LWKSKLETAI ASHQQAMEEL KVSFSKGVGT ETAEFAELKT QIEKMRLDYQ
QEIENLQNKQ DSERSAHTKE LEALRAKLMQ VIKEKENSLE AIQSKLDKAE EQHLVEMEDT
LNKLQEAELK VKELEVLQAK CNEQTKVIDH FTSQLKAAEE KLSDLDALQK ASSEGKLEIE
NLRQQLEAAE KQIKNLEIEK DAESSKASSI TKELQGKELM LNNLQENLSE VSRVKEALEK
ELQTLKEKFA DASEEAVSFQ RSMQETVNKL HQKEEQFNAL SSELEKLREN LTDMEAKFRE
RDEREEQLIK AKEKLENDIA AIMKMSGDNS SQLTKMNDEL RLKERNVEEL QLKLTKANEN
ASLLQKSIGE VTLKAEQSQK EAAKKHEEEK KELLRKLSDL EKKMEMSWNE CQDLKARYEE
ASSESRAKHE EVLQNLHKLL RDTEERLKAA QEENRELLQK LEELGKQADR ARAAQTAEDA
MQIMEQMTKE KTETLASLED SKQTNEKLQN ELDTLKENNL KNVEELNKSK ELLTVENQKI
EEFKKEIETL KQAAAQKSQQ LSALQEENVK LNEELGRSRD EVTSHQKLEE ERSVLNNQLL
EMKKRESKLI KDADEEKASL QKSISITSAL LTEKDAELEK LRNEVTALRG ENASAKSLHS
VVQSLESDKV KLELKVKNLE LQLKENKRQL SSSSGNTDTQ AEEDERAQES QIDFLNSVIV
DLQRKNQDLK MKVEMMSEAA LNGNGDDLNN YDSDDQEKQS KKKPRLFCDI CDCFDLHDTE
DCPTQAQMSE DPPHSTHHGS RSEERPYCDI CEMFGHWATN CNDDETF
//
