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Database: UniProt
Entry: A0A3B4DQ33_PYGNA
LinkDB: A0A3B4DQ33_PYGNA
Original site: A0A3B4DQ33_PYGNA 
ID   A0A3B4DQ33_PYGNA        Unreviewed;      1487 AA.
AC   A0A3B4DQ33;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 1-B-like {ECO:0000313|Ensembl:ENSPNAP00000025221.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000025221.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000025221.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_017540975.1; XM_017685486.1.
DR   STRING; 42514.ENSPNAP00000025221; -.
DR   Ensembl; ENSPNAT00000008148.1; ENSPNAP00000025221.1; ENSPNAG00000010194.1.
DR   GeneID; 108413125; -.
DR   CTD; 402833; -.
DR   GeneTree; ENSGT00950000182975; -.
DR   OMA; WPEVANS; -.
DR   OrthoDB; 2918432at2759; -.
DR   Proteomes; UP000261440; Unplaced.
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; 1.10.418.10; Calponin-like domain; 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:SF3; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 1; 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}.
FT   DOMAIN          235..350
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1352..1486
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          422..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          893..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1193..1285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          811..841
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        422..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..672
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1070
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1487 AA;  165326 MW;  0349594179120B15 CRC64;
     MDVGAAGGVD GGPRRADSVE GGLEIIPLEL YDSARAKIDA NLRWLFAKAY GEAHVPADLR
     DPFYTDQYCV EHIKPPVLTL LLSSELYCRV CVLLLKGDQT ASLSSHQSVL QALARHGIYA
     REPDDTPVTH DDLSSTPIKM SSHIPLIDAL MLAWTVEMMS IERVVSSVKR FSTFSASKEL
     PFDVEDAMLF WINKVILKTR EISEKELKLK QHLMESPCHQ KPDFMHALAH CMLEPVELSR
     VVRYRRDHLS GRCLPHMPLV EDLMKDICDG AALLTVIHYY CPDFMRLEDI CLKEVLSISD
     SVYNIQLLRE FSNEYLDRCL YLRPEDLLYA PPVLKHNVMV FIAELFWWFE VVRPDFVKPR
     DPQEIKEARA SVQAKSSRPL VPISNATKRS FLSTSPSVDS MVSGSAHDTC IRYYLHPEES
     ASTSVTKVSP SHSPSHPLLP LRQRQQKPVQ GEETAEFRNR SSSLSRMDGH SPGSRLAWME
     RRQRPLSQME MEWERLCGDN ISLARSISKD SLASNVVSIT PRHHINGQPL PHTACSHDFE
     DQEEELVAVI SSGGVATFRE SRPESFFLEP LQPAVLRPNK EKSVVVSKRD ESGEGRGQRR
     RAVHTPTEHT AINQTFTTVS TVEPEGSPQS GGFFLHGKSE CVRSSPVGVW VGGVSDSEFE
     EEEEEAEDDD VEERDIAKAH IRKLLGHGQE EEESAKLREE VRGREREDKE GASGRSSPCP
     STLSQASSTS TGAGHTRQSS PCRSTFSQAS SASSRMTSFA ERRLHRAVTP DGFYSGCSSQ
     TSTPDGSESA PFPPQAGDRA SPSPGARGGV ASELIHLRMQ LEEKRRAIET QKKKMERLSA
     RQRLKLGKAA FLHVVKKGRG DTLPRPVKQE VLKEKETEKE MAKDDSYVEA LKAKAKAKET
     EPSPDKESRQ LAEISAAPPA TLEVDNRVSE GEAWEEGGGE LDLSECNRSI ELLNEAIGSI
     QQQMMQLSVQ QDLLMRQTAL SPTQEKPQSP SEPNEPKLRP SVQFVEISTA TRRPPKLSSG
     RTPRTKPAEL KLSKGSKVNT GDPRPSPVSR TPRAENEEDG VSKDVGDKAN GRSLARSLAR
     NATFRLHDAA NRRTDGPESP KAEPPTVEPS QAEPGRERSG SGGSGKENVP VPCEENRTKG
     QLIEVDLSDL TNPESSAEPE GEQKSGLGFF FKDDQKAADE LAKKRAAFLL KQQKKAEEAR
     LRKQQLEAES ELKRDEARRK AEEERVRKEE EKARRELIKQ EYLRRKQQEL LEEQGVAKPR
     PRHRKPRPKS LHRRESGNAT PVGLCAAPSG SSLSLASAAT EADSITSGGG SQRGESVESF
     PMLSRNASRN VERDWDNGST ASSVTSVAEY NGPRLFKEPS AKSNKPIIQN AIAHCCLAGK
     VNEAQKNAIL EEIERCESNH LMILFRDGGC QFRALYAFAP DTEEILKLVG TGPRAITRKM
     IDKLFKYSSD RKQFTVIPAK TVSVSVDAIT IHNHLWQVKR PGSSKRK
//
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