ID A0A5C6MX85_9TELE Unreviewed; 1539 AA.
AC A0A5C6MX85;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 3 {ECO:0000313|EMBL:TWW58948.1};
GN ORFNames=D4764_06G0004780 {ECO:0000313|EMBL:TWW58948.1};
OS Takifugu flavidus (sansaifugu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW58948.1, ECO:0000313|Proteomes:UP000324091};
RN [1] {ECO:0000313|EMBL:TWW58948.1, ECO:0000313|Proteomes:UP000324091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW58948.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TWW58948.1};
RA Xiao S.;
RT "Chromosome genome assembly for Takifugu flavidus.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000256|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000256|PROSITE-
CC ProRule:PRU00841}.
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:TWW58948.1}.
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DR EMBL; RHFK02000019; TWW58948.1; -; Genomic_DNA.
DR Proteomes; UP000324091; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0036449; C:microtubule minus-end; IEA:TreeGrafter.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IEA:TreeGrafter.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:TreeGrafter.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:TreeGrafter.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR FunFam; 3.10.20.360:FF:000001; Calmodulin-regulated spectrin-associated protein 3 isoform 2; 1.
DR Gene3D; 3.10.20.360; CKK domain; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595:SF2; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 3; 1.
DR PANTHER; PTHR21595; PATRONIN; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50346; PRC-barrel domain; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000324091}.
FT DOMAIN 226..336
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1389..1523
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 193..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..692
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..887
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..957
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1246
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1301
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1539 AA; 168204 MW; C7847D888253AAA6 CRC64;
MVDSPGAMNK VSTVAEIKPL DQYDFSRAKI CASVRWLLSK SYGSAENVPV EMREPLYKDQ
YDQEHLKPSI NKLLVSPEIY CQAHVLLAQV HGVSASPSQA SPADAEALLQ LLEKKGLAPK
VQDADVTQED LRCVPIRMKA HLAMIDALMT LAAKEIVDQV KMAAEAEQIG AGAPWENALL
FWVNRLNQKL RELTEEEEEP PRPQTCSDVQ PAQDAQCPSS RWYWKLVPIR YRKDKVQSKL
TPTFPLIHGV KDLSNGCAIA SVLHYYCPVL LPLEDVCLKD TMSVADSVYN LQLIREFCES
SLQSCCPLAV EDLLYAPPPL HLNIMSFISE LLHWFEVKKP DFVQPVQATD LTDVSGLLDC
TSPINGSGNS GSPSFILKQP FMPITSPVSP ENKCWTKKQI SRPLSAVTFS IPFGLDSDVD
IVMGNPIDSV FRSASTDTGI PAMTTPVSSG GANHVPYSPP EDISHLVSSS VPLQCSSWGP
YAHTTPLGEL PTIEEALKVA HGPGSKERRK GNAAGKGGRP EARLRPEGAP AGFFLHSPEE
ENPQLSSSAP CRSGVLHRPV GGEGVDGKRQ GRGERRERSG CAPDMSRDDD SVLRDGSVDS
SEASDDGPRN APGNMRPSKG HHGNQSAGNS PRMTSFAERR DNRRRHPAAS GEEVASAPTP
TTPGTPHTPS TPAGAPGRQD SPGPRGPEPG SEAWELGVRL EEKRKSIEAQ KRRIEAIFAK
HRQRLGKTAF LQLKRQQGEG GGGGGAEDNL TLEERLTRME EQLKQEEEKE EKDKEKDGAQ
EKDKPSALTP PRLEKQVTFS IESKKEAETK KAAEKGGEVM LVEYNEVVQK LSEALQSLQK
DMQKLTEQQQ QLMSNQRPRN TPKNAPRTSA KKPGTPPQTP TRTPPRTPTK TPTRNTSKAW
MIPPGSNPKS TSPSQHSQVL TSPKTAISSS CPAPRTKIQS TTPRSPKHHP RPQHQPHPRP
SELKFPPLNR MLTPTHNVDT LPHLRRVSPS KCQVQTSSSF RIGGPQTPKE SPQPVQPIQP
PQADECPSET GSSDTPTQFS MELEQDEAVG GLPVLLHPRQ DRPRAADGSS SGAPSECSFE
SETFSISAAY SRGGDAGRGV SAGTHRYEVS DEQTDEGREF SSDSMSDHTE SAVEPARRPA
AAALDPTEQL DLAMEAINTP EQPAEPKEEQ MGLTAGPSAE QNESGAKGRI HFFFTEDVQN
EEEMAQRKAL LLEKQQRRSE ELKKRKQWHE RERENSTPPV GTTSPSATPP ATPARRGGFT
RAEYARRQQL RIMDDLDKML QQKSASQVRN PAKKARSRPR SMTREETRLS LSPAKTTTGS
KLAKVHSHSS VNLAATEEPR NKSDGPSKKA NSRPNSPACM TPSKLTNPNG DKEWDTGSNG
TSPAPEYTGP KLFKEPSFKS NKFIIHNALS RCCLAGKVNE TQKNKIVEEM EKSDANHFLI
LFRDASCQFR GVYTMNSDSQ ELVRLAGVGP RTIGSTQVES MFKYSSDRKQ FSTIPSKTMG
MSVDAFTIPS HLWQGGGGVA GAGGGSRRAS INKKAVASK
//
