ID   A0A3Q2G912_CYPVA        Unreviewed;      1405 AA.
AC   A0A3Q2G912;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=CAP-Gly domain containing linker protein 1 {ECO:0000313|Ensembl:ENSCVAP00000020505.1};
GN   Name=CLIP1 {ECO:0000313|Ensembl:ENSCVAP00000020505.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000020505.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000020505.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   Ensembl; ENSCVAT00000014164.1; ENSCVAP00000020505.1; ENSCVAG00000001958.1.
DR   GeneTree; ENSGT00940000155122; -.
DR   Proteomes; UP000265020; Unplaced.
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   InterPro; IPR005491; ENT_dom.
DR   PANTHER; PTHR18916:SF10; CAP-GLY DOMAIN-CONTAINING LINKER PROTEIN 2; 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   SUPFAM; SSF90257; Myosin rod fragments; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 2.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
DR   PROSITE; PS51138; ENT; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT   DOMAIN          75..117
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   DOMAIN          227..269
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   DOMAIN          655..746
FT                   /note="ENT"
FT                   /evidence="ECO:0000259|PROSITE:PS51138"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1320..1342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          343..601
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        122..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1405 AA;  156572 MW;  45100E38AEAC212F CRC64;
     MSTAKPTGIK APSKIARAQG TGAPKTNPPT AKAAVADKAA VLGSGGDGKN AEDVFQIGER
     VWVNGNKPGY IQFLGETQFA PGQWAGIVLD EPIGKNDGSV AGVRYFQCEA LRGIFTRPSK
     LSRTEGEANG TQTAPPSRAA SPTPSVGSVA SQTPAAKSTV PSSSTATKKA SSATPAAAAS
     SNLAQTNSES VSNLSESGSV KKGERELKMG DRVLVGGTKA GVVRFLGETD FAKGEWCGVE
     LDEPLGKNDG AVAGTRYFQC QPKYGLFAPV HKVTRIGFPS TTPAKAKTTA RKVVATPSGL
     KRSPSASSIS TMSSVASSVS TKPSRTGLLT ETSSRYNRKI SGTTALQEAL KEKQQHIEQL
     MGERDMERAE VAKANSHVGE MQQEISLLRE DQEQMEAKMD QLRSLVEAAD KEKVELLNQL
     EEERRKVEDL QFRVEEACIT KGDLETQTRL EHAHIKELEQ SLLFEKTKAE KLQRELEDTR
     VATVSERSRI MELERDLSLR TREVADLQLR LGMQQNSEDS NATLSPLLEE INSLRDQLSA
     QETKQKEEME KYKEKLEAQE KAHSEAVAQL QATCVLLSSE KEQLQMRLSQ AEKDNADTVE
     LWRSKLEATV ASSQQAMDEL KVSYSQGAGA QMEELAETKS ALEKLKLEHR LALEEAAAKH
     KANASALTET VQALKAQLSA VTEEKERLEE SLRSSVEKVE EQHLVEMEDV LGKLHAAEIR
     VKELEEQQAK LAQQFQDKDT ETKEKRGEMA SLRSQLAQSN QECAALKSRL EELQNQGESN
     GAKVGELSSQ LENKEQEVAS LQETLTALKQ QKESMSKEIE SLSQRLLDST EELNKSAQTM
     QETLEKLGKK EEQCTSLTNE SESLRSQLAG MERKLKASDE KLEQFSKDKS KLEKDISDMM
     KASGDSSDQL TKMNEDLMQK ERRLEELQNQ LAEEKEKVAH LDEKLLKEQS NKEQQLREAK
     DAHQSETSSL QEKIVALENS LKQSEIRVED LKASQEQSLS EASELHLKEL EVLQTQIDKL
     KLELLTSNNR TEELEKTVGE LQPYKEQAQA KEGSDKSAEV LEQLTKEKEV LLKERNEANA
     LLKELQNSKE DIQTQLEALR KENSKYQEDL DSSKEQLCTE TQKTKSLCLE IEELKEAVSV
     RSESLQRLQD ENSRLSQELE NHHKDQGTHS NLQKELEELK ESEATLKQQL SSEKAALQHS
     IHKNSALVAE RDQQVENLKS ELVAMREESA SIKTLQKTIQ ALEEQRSNLQ DRIKRLEKDL
     TARPDNINQT SGDAVLDKLR EDKETAENQI EFLNSVIVDL QRKNGELKDK LEKMAAAALN
     GNNPSEMDNS YEEQPAKKKP PPRKFCDICD CFDLHETEDC PLQEQIEDSP PHTTYHGSKG
     EERPYCDTCE VFGHWTESCT DDQTF
//