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Database: UniProt
Entry: V9KJ51_CALMI
LinkDB: V9KJ51_CALMI
Original site: V9KJ51_CALMI 
ID   V9KJ51_CALMI            Unreviewed;       686 AA.
AC   V9KJ51;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1 {ECO:0000256|ARBA:ARBA00040932};
DE   Flags: Fragment;
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO98110.1};
RN   [1] {ECO:0000313|EMBL:AFO98110.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AFO98110.1};
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CALCOCO family.
CC       {ECO:0000256|ARBA:ARBA00037963}.
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DR   EMBL; JW865593; AFO98110.1; -; mRNA.
DR   AlphaFoldDB; V9KJ51; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.2840; -; 1.
DR   Gene3D; 6.20.250.40; -; 1.
DR   InterPro; IPR012852; CALCOCO1-like.
DR   InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR   InterPro; IPR041611; SKICH.
DR   PANTHER; PTHR31915:SF5; CALCIUM-BINDING AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR31915; SKICH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07888; CALCOCO1; 1.
DR   Pfam; PF17751; SKICH; 1.
DR   Pfam; PF18112; Zn-C2H2_12; 1.
DR   PROSITE; PS51905; ZF_UBZ1; 1.
PE   2: Evidence at transcript level;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01253}.
FT   DOMAIN          648..674
FT                   /note="UBZ1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51905"
FT   REGION          512..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          138..256
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          285..322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          411..484
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        532..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFO98110.1"
SQ   SEQUENCE   686 AA;  78047 MW;  770C0955BF710380 CRC64;
     LYIPGTSVEC HYSLAPHARW TSKDWIGIFK VRWSSVRDYH TFLWSPSPDG YAEGSPTNCS
     VRFQASYLPR SGPTLYQFCY VEFKGEVAGV STPFTFSDPK PEEDFITLED FENNSDMLVV
     MTKTSLLERQ LEESDRTKES LVARQRHLEG EMQQLQGKIE ELEQALEIAI AEQTRLNQET
     HSLEEEKQRV TTQHISLEQE HAQAIDRIQE LEEDIQALSG TVLEKESELE RMKERIKKLL
     LQREQQSTRL EEEAEEKGFY QSHSEASQLE VQRLQGEQQV LRNALADTDS LVTELRDEVE
     DLQQKASAAH ELKGQVDILR EQLRCTHDQL AASQQKVVLM GEEMGSASST RDRTMSELHR
     SRLDVADLNI RLAEVTVKWK ESKGQWLKEK AIFLQSSEAE KERVLKLSVE LVKVKSSLQE
     QESEAENLRL ELIRERDCSR VQLSELLRER KEMKSGFRVV EKEKEKLQEE KQELLEYVKV
     LEARLEQIPG PNDSDATYKE ASAITEVADG AEDVECAPIT PSEGRGRPKL SSYSLCDNTN
     SQDSLTFSTP PLSPQELNSQ VVISQPMAIS PQHNPAPHDS SSESEDEEAG GVYSEATPSQ
     SDGLNALLTE LGHTLHFEVS SCRGLPPRSQ HEALDRDQAE ESTAASLWKE CPICKQHFPS
     EYKNQALEDH IDSHFFFSTS DPFTFE
//
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