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Database: UniProt
Entry: G3PQR3_GASAC
LinkDB: G3PQR3_GASAC
Original site: G3PQR3_GASAC 
ID   G3PQR3_GASAC            Unreviewed;      1462 AA.
AC   G3PQR3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Calmodulin regulated spectrin-associated protein family, member 2b {ECO:0000313|Ensembl:ENSGACP00000019948.1};
GN   Name=CAMSAP2 {ECO:0000313|Ensembl:ENSGACP00000019948.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000019948.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000019948.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000019948.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   STRING; 69293.ENSGACP00000019948; -.
DR   Ensembl; ENSGACT00000019986.1; ENSGACP00000019948.1; ENSGACG00000015109.1.
DR   eggNOG; KOG3654; Eukaryota.
DR   GeneTree; ENSGT00950000182975; -.
DR   InParanoid; G3PQR3; -.
DR   OMA; YRGLYTW; -.
DR   TreeFam; TF315529; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000015109; Expressed in diencephalon and 9 other cell types or tissues.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR   GO; GO:0031175; P:neuron projection development; IEA:InterPro.
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:SF5; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 2-LIKE ISOFORM X1; 1.
DR   PANTHER; PTHR21595; UNCHARACTERIZED; 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, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW   ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT   DOMAIN          234..345
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1325..1459
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          511..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          739..769
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        511..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..1011
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1059
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1078
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1285..1301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1312..1326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1462 AA;  162105 MW;  101FE41A19795EE9 CRC64;
     MGDAAEDIIL RGMRRTFIVP SIKSFDHYDF TRAKISCSLT WLVAKAFGSD AVPEELAEPL
     YRDQYNQEHL KPPVACLLQS AELYCRAGSL ILRSDAVKPL LGHNAVIQAL AQKGLYVTDQ
     DRLVTERDLA STPIHMSSHL ALIDTLMMAY TVEMVSVERV MTCINRCSSA EPSHMDGHLQ
     ELPYDTEDAI HTWINKVNEH LRDILVEEQK LREASPQESD ATTHKSPCKW YWRLVPARYR
     KDHAQQMSAP SLPLVENLLK DNTDGCALTT LLHFYCPQAI RLEDICLKET MSLADSLYNL
     QLVQEFCRDN LNHCCHFSLE DMLYAHASIK SNYLVFMAEL FWWFEVVKPS FVQPRVFDPD
     GTVQVQNNLS MLLLAPIKQS YADGPDSPDN APAQVEKGDL IHAIRSYSVS ATGIMKRSAS
     MSYVDGCVGT WPKEKRSSCR GISFEIPLVG DPTVLPGEAP ALGGMTRSAS SDGLGFKVHY
     ASRGGMKRHL SLMPVNVNGQ GRHIAEEANR DFKQSSVNLP KSVPRYSNGV FPESNHHGNR
     RSHISPSTPP SIEEALKIIH DTERPHASLG VGDGDNGFFL HGTEPPDPTD ASGAKGQGDE
     QDEVDTGIHV RTEDIQSLDE DSSSLRDYSD IDPDCEAVTR SCPLPEQSVG DGSERGSPCP
     SSAPTIQRSH PGSPASSSGG SGGGVVRMTS FAEQKFRKLE GRSSGGTTPE SSDLNVPYTQ
     LPKSISFQPS PRDPSHLIAT EMIQLRMKLE EKRRAIEAQK KKVEAAFTRH RQRMGRTAFL
     NVVRRKGITA PLSPSAAEAP SPEPPTASKE SNQGSMERAE RCKPDGAAPK SPCEEGGGQN
     HMTLTRVSDT GTSPGEIDLT EYTRSIERMN TSLGFLQTEM QRLAQQQEKI MSMREEQQQS
     WVIPPPAPSP HRQLRELRSS SVTGRGSGRG SVGSLSPILS SSGSPRPPNR SPAGIKRRPA
     SFHARTPRTP RPNDLKVTPF SRMLNTQTSV DSLPRLRRFN PSQNQNSSFA YLGHDEGPLE
     GQNQEAKDHR ENTKDKEDLL SAKEAAKEKE DERQKERTGE VQPASSSEVL SQPVSEIQRP
     TGGRVREQPQ DRRHLVEVTL SGLKPPGGRP GGPETGGGEG DVEAGGDPLG KDQKMCCGFF
     FKDDVKAEED MAAKKAFLLE KRLRREKETQ EKKQQQEVDH EQKREAARLK ADEDQQKKDQ
     EKARREYIKQ EFMRRNQLKL MENVDEVTKP RSGSLKKKPR PKSIHRDVME SLTPPVRATG
     FSVSSISLAS LNLADDDQPN NRKNNRPDSA EGFSSCPSTG SRNEEKDWEN DSTTSSTPSN
     NEYTGPKLYK EPSAKSNKYI IQNALAHCCL AGKVNEGQKN KILDEMEKSE ANNFLLLFRD
     AGCQFRSVYA YCPETEEITK LAGIGPKSIT VKMIEGLYKY NSDRKQFSLI PAKTMSASVD
     AITIASHLWQ TKKQATPKKL HA
//
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