ID A0A3Q1NN83_BOVIN Unreviewed; 1403 AA.
AC A0A3Q1NN83;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE SubName: Full=CAP-Gly domain containing linker protein 1 {ECO:0000313|Ensembl:ENSBTAP00000074178.1};
GN Name=CLIP1 {ECO:0000313|Ensembl:ENSBTAP00000074178.1,
GN ECO:0000313|VGNC:VGNC:27444};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000074178.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000074178.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000074178.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000074178.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000074178.1};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR Ensembl; ENSBTAT00000068963.2; ENSBTAP00000074178.1; ENSBTAG00000016779.7.
DR VEuPathDB; HostDB:ENSBTAG00000016779; -.
DR VGNC; VGNC:27444; CLIP1.
DR GeneTree; ENSGT00940000155122; -.
DR OrthoDB; 5412539at2759; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000016779; Expressed in semitendinosus and 108 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q1NN83};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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 128..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 1067..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..377
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1403 AA; 157854 MW; 80F599420B833483 CRC64;
MSMLKPSGLK APTKILKPGS TALKTPAAVA APIEKTISSE KASSTLSSET QEEFVDDFRV
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CELLKGIFTR
PSKLTRKVQA EDEADGPQTP HASRATSSLS 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 LKAAEEKLSD LDALQKASSE GKLEIENLRQ QLEAAEKQIK NLEIEKDAES
SKASSITKEL QGKELMLNNL QENLSEVSQV KEALEKELQT LKEKFADASE EAVSFQRSMQ
ETVNKLHQKE EQFNALSSEL EKLRENLTDM EAKFRERDER EEQLIKAKEK LENDIAAIMK
MSGDNSSQLT KMNDELRLKE RNVEELQLKL TKANENASLL QKSIGEVTLK AEQSQKEAAK
KHEEEKKELL RKLSDLEKKM EMSWNECQDL KARYEEASSE SRAKHEEVLQ NLHKLLRDTE
ERLKAAQEEN RELLQKLEEL GKQADRARAA QTAEDAMQIM EQMTKEKTET LASLEDSKQT
NEKLQNELDT LKENNLKNVE ELNKSKELLT VENQKIEEFK KEIETLKQAA AQKSQQLSAL
QEENVKLNEE LGRSRDEVTS HQKLEEERSV LNNQLLEMKK RESKLIKDAD EEKASLQKSI
SITSALLTEK DAELEKLRNE VTALRGENAS AKSLHSVVQS LESDKVKLEL KVKNLELQLK
ENKRQLSSSS GNTDTQAEED ERAQESQIDF LNSVIVDLQR KNQDLKMKVE MMSEAALNGN
GDDLNNYDSD DQEKQSKKKP RLFCDICDCF DLHDTEDCPT QAQMSEDPPH STHHGSRSEE
RPYCDICEMF GHWATNCNDD ETF
//
