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Database: UniProt
Entry: A0A7K8EQE3_LEURO
LinkDB: A0A7K8EQE3_LEURO
Original site: A0A7K8EQE3_LEURO 
ID   A0A7K8EQE3_LEURO        Unreviewed;      1434 AA.
AC   A0A7K8EQE3;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   18-JUN-2025, entry version 18.
DE   SubName: Full=CLIP1 protein {ECO:0000313|EMBL:NXB53452.1};
DE   Flags: Fragment;
GN   Name=Clip1 {ECO:0000313|EMBL:NXB53452.1};
GN   ORFNames=LEUROT_R00027 {ECO:0000313|EMBL:NXB53452.1};
OS   Leucopsar rothschildi (Bali myna) (Rothschild's mynah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Sturnidae; Leucopsar.
OX   NCBI_TaxID=127929 {ECO:0000313|EMBL:NXB53452.1, ECO:0000313|Proteomes:UP000522331};
RN   [1] {ECO:0000313|EMBL:NXB53452.1, ECO:0000313|Proteomes:UP000522331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-002-02 {ECO:0000313|EMBL:NXB53452.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXB53452.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NXB53452.1}.
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DR   EMBL; VZTC01009120; NXB53452.1; -; Genomic_DNA.
DR   Proteomes; UP000522331; Unassembled WGS sequence.
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:UP000522331};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          79..121
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   DOMAIN          233..275
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          349..376
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          402..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          569..1212
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1238..1296
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1320..1369
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        25..49
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..163
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..331
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXB53452.1"
FT   NON_TER         1434
FT                   /evidence="ECO:0000313|EMBL:NXB53452.1"
SQ   SEQUENCE   1434 AA;  160914 MW;  165C9BF14100968E CRC64;
     MSMLKPSGLK APSKTIKHGG SLLKTPAPVA AAPAEKAAPS EKSSSTAPAD AHEEFVDDFR
     VGERVWVNGN KPGFIQFLGE TQFAPGQWAG IVLDEPIGKN DGSVAGVRYF QCEPLRGIFT
     RPSKLTRKVV TEDEANGTQT AHASRATSPT STSAASVVSS TAALPPSGIP QKSPLAAKEH
     ATPSQISNLS KTASESISNL SEAGSLKKGE RELKIGDRVL VGGTKAGVVR FLGETDFAKG
     EWCGVELDEP LGKNDGAVAG TRYFQCQPKY GLFAPVHKVT KIGFPSTTPA KAKPAVRKVL
     PTPTALKRSP SASSLSSLSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
     QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALVRDGHDR HVLEMEAKMD QLRAMVEAAD
     REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLETQTKL EHARIKELEQ SLLFEKTKAD
     KLQRELEDTR VATVSEKSRI MELERDLALR VKEVAELRGR LDSSKHIDDV DTSLSLLQEI
     SSLQEKMAAA GKEHQNEVNS LKEKFGLSEE ALQKEIKALS ASNERIAKEN ESLKTKLDHA
     NKENSDVIEL WKSKLESAIA SHQQAMEELK VSFSKGVGAQ TAEFAELKTQ IEKMKLDYEN
     EMANLKLKQE NERSHHLKEV ESLKAKLVAV TEEKEQNLES LKTKLESVED QHLVEMEDTL
     NKLQEAEIKV KELEVLQAKY NEQTKVIDSL TPQIKAAEEK LLDLAALEKA NSEGKLEIEK
     LSKQLEAAEK QIQTLETEKG DGISQASNLA KELQGKEQKL LDLEKNLSAV NQVKDSLEKE
     LQVLKEKFTN AADEAENVQQ AMQETVKKLN QKEEQFALMS SELEQLKSSL TEMERKLRER
     EEREQQLMEA KAKLENDIAE IMKSSGDSSA QLTRMNDELR LKERQLEQIQ LELTKANEKA
     AQLEKNVEQT TQKAEQSQQE TLKIHQAELK TLQDQLTDMK KQIETSQHEY KDLQAKHEKE
     TSELVAKHDA DIQGFKQNLL DAEEALKSAQ RKNSELEAQA EELQKQAEQA RVAKLAEDVF
     QAVEQVTKEK DAIHKEKIET LASLENSRQT NQKLQNELDM LKQNNLKNEE ELNKSKELLN
     LENKKVEELK KEFEALKLAA AHKSQQLEAL QEENVRLAEE LGRSRDEVSS QHHKLEEERS
     VLNNQLLEMK KRESTLKKEI DEERASLQKS INVTSALITQ KDEELEKLRH EITVLRGENA
     SAKTLQSVVK SLESDKLKLE EKVKNLEQKL KENNEQPLTV MSPSGKVRAT PEELAREKQI
     DFLNSVIVDL QRKNEELNLK IQRMCEAALN GNEEEINNYD SEEESLSKKK PRLFCDICGC
     FDLHDTEDCP TQAQALEEPP HSAHHGSRRE ERPYCDTCEV FGHWTADCND DETF
//
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