ID A0A3P9MYC4_POERE Unreviewed; 1508 AA.
AC A0A3P9MYC4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 1-B-like {ECO:0000313|Ensembl:ENSPREP00000002362.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000002362.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000002362.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000002362.1};
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 Ensembl; ENSPRET00000002410.1; ENSPREP00000002362.1; ENSPREG00000001740.1.
DR GeneTree; ENSGT00950000182975; -.
DR OMA; HIRIEDE; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000001740; Expressed in head.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd22265; UDM1_RNF168; 1.
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};
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:UP000242638}.
FT DOMAIN 196..311
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1373..1507
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 365..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 168742 MW; 3C52031CE202ABC4 CRC64;
MVIREAVKTR EIQMSRHCDC FPDHIPSDLR DPFYTDQYEQ EHIKPPLIHL LLSGELYSRV
CGLILPTEQA AYLQSHQSVI QALSRKGIYV LEINGTPVSD MDLSSSPIKM SAHIHLIDAL
MMAHTVKMIS IEKVVSCVKR FSNISASKEL PYDLEEAMIL WINKITTKMR ELTEKECKVK
QHFLESPSHH KSPSKWYWKL VPVRYRRDHL SGRTLQHFPL VEDILKDVSD GTALLAVIHF
YCPEVVKLED ICLKDVPSIA DSMYNIQLLK EFSNEYLNEC FFLNTEDLLY SPPVLKNNVM
VFIAELFWWF ENMKPDFVRP RDLQDVKDVR ALLQPKNSRS YVPVSNVTKR SFMPSSNTVD
ILTTTSTKDQ SATSTSSPSH SLLPLRQRQQ NVVEKSTSDL RKRPDSMART DGQRQDSIVA
WPERRTRPVS QPVPYAVHFA KEDNADSLSL VRTISKDSLA SNIMSITPKH MLGSSLPQHR
LSGQSLLSHM RIEDEEEEIE EEELVSVIHP SAFPRHRIGS DMEQDELEAQ KLTSSARASD
VFRHDASPFA LDRQTDGYYL EPLMPTIPKP AKEKGISLNK QEESGESRSR AVAAKTRTEN
IPFSSKKKHC VVDSVLSSSR PHTDGPVGSS EHPGFFLHLA AEPEKTPHTT EAGHDSDSDI
ADLEEDDEDD QTELEKTLRG NRLVEGYIAG FGDGEIESAK LREDLKVSEH EDKEDASGRS
SPCPSTVSWA SSCSASGSAG IKMTSFAERK LLKLGLRDGC SSTSSSQKTT PDGSEVPPQW
QAKETSTMIG KNVTAGPVVP SQLLQLHMQL EEQRRAIEYQ KKKMEALNAK QRLKLGKAAF
LNIVKMGGGK SDTLPLPVRH SLDSSGSTAA ERRKAKTQAC KDDSCLDSLK SQTDGWTMTR
DNSWNTLTQD NSAEPDFNEC SNSIDLLNQA ISSIQQQMLQ LSLQQDFLMK QSVASPPDHA
QTEKSTDSGI DPNTPQTASS TSDSRSFAVH FVDIGGSSLV PFRRPPKLSS SQRSKAAERK
QNKANNKSVL TKSTDPIPGS DTSSRGRNDG ELETAEVQRV QRNSTFRVHE SNGDRDVQLS
DKLKSQDPAV VTKTSESASQ DARQEEEQAT NCSKQNVDID ESGRVKSQLI EVDLSELKDP
VEDGGADITD GTAEGEQKGG LGFFFKDDEK AEDEMAKRRA AFLLKQQRKA EEARLRKQQQ
EAESEIKRDE ARRKAEEDRI RKEEEKARRE LIKQEYLRRK QEALMEEQGL VKPRTKTKPR
GNRPKSMHRG YSSSLPKGST TRDSLKVSML MKNRRSGAAS RGADLSFSHR GSTLSLATDA
DSVISGGADS NRAASVCSVD SFPMLSRASS RNMDRDWENG SIASSVTSVE YNGPKLFKEP
SSKSNKPIII NAIAHCCLAG KVNEVQKNIT LEELEKCESN HLFILFRDGG CQFRAIYTYS
PDTEVIVKYM GIGPRVITQK MIDKLYKYNS DRKQFTVIPA KTVSVSVDAL TMHNQLWQIK
RPGSARRK
//