CAM1B_DANRE
ID CAM1B_DANRE Reviewed; 1558 AA.
AC A5WUN7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 1-B;
GN Name=camsap1b; ORFNames=si:dkey-157g20.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization. Specifically recognizes growing microtubule
CC minus-ends and stabilizes microtubules. Acts on free microtubule minus-
CC ends that are not capped by microtubule-nucleating proteins or other
CC factors and protects microtubule minus-ends from depolymerization. In
CC contrast to camsap2 and camsap3, tracks along the growing tips of
CC minus-end microtubules without significantly affecting the
CC polymerization rate: binds at the very tip of the microtubules minus-
CC end and acts as a minus-end tracking protein (-TIP) that dissociates
CC from microtubules after allowing tubulin incorporation. Through
CC interaction with spectrin may regulate neurite outgrowth.
CC {ECO:0000250|UniProtKB:Q5T5Y3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of
CC microtubules. In contrast to camsap2 and camsap3, does not form
CC stretches of decorated microtubule minus-ends.
CC {ECO:0000250|UniProtKB:Q5T5Y3}.
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
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DR EMBL; CR396583; CAN88213.1; -; Genomic_DNA.
DR EMBL; CT971581; CAN88213.1; JOINED; Genomic_DNA.
DR EMBL; CT971581; CAN88254.1; -; Genomic_DNA.
DR EMBL; CR396583; CAN88254.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001093471.1; NM_001100001.2.
DR AlphaFoldDB; A5WUN7; -.
DR SMR; A5WUN7; -.
DR STRING; 7955.ENSDARP00000118745; -.
DR PaxDb; A5WUN7; -.
DR PeptideAtlas; A5WUN7; -.
DR PRIDE; A5WUN7; -.
DR Ensembl; ENSDART00000147707; ENSDARP00000118745; ENSDARG00000035122.
DR GeneID; 561094; -.
DR KEGG; dre:561094; -.
DR CTD; 561094; -.
DR ZFIN; ZDB-GENE-070705-301; camsap1b.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR InParanoid; A5WUN7; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; A5WUN7; -.
DR TreeFam; TF315529; -.
DR PRO; PR:A5WUN7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000035122; Expressed in early embryo and 24 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
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; PTHR21595; 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; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT CHAIN 1..1558
FT /note="Calmodulin-regulated spectrin-associated protein 1-
FT B"
FT /id="PRO_0000316830"
FT DOMAIN 231..346
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1421..1555
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 400..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1360..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 849..887
FT /evidence="ECO:0000255"
FT COILED 971..1004
FT /evidence="ECO:0000255"
FT COILED 1243..1303
FT /evidence="ECO:0000255"
FT COMPBIAS 402..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1558 AA; 173900 MW; 335B4B3BBEE05F46 CRC64;
MEDGGLGMDA ELGADSARRK MEAAGEALEI VPLEMYDSAR AKIAANLRWL FAKAFGIDHI
PEDLRDPFYR DQYEQEHIKP PVIRLLLSCE LYCRVCALIL KGDQVASLQS HQSVIQALSR
KGIYVMEDDD TPVTDSDLTC QPIKMSSHIP MIDALMMAYT VEMISIEKVV SCVKRFSTFS
ASKELPFDLE DAMIFWINKV NLKMREITEK EHKSKQHLLE SPSHQKSPSK WYWKLVPVRY
RRDHASGRQL PYFQMLEDLI RDVCDGAALL TVVHYYCPEL MKLDDICLKE VTSIADSLYN
IQLLKEFANE YLNKSFYLTL EDLLYAPPVL KHNVMVFIAE LFWWFEIVKP EFVQPRDVQE
FKDARAVSQP KSARPTVPIS NATKRSFLVS PGAADPVLPV QNSPEVCNSN KGSSGFSPSH
PLLPLRQRQK KAQPAEESTA CRNRSNSLTQ EGHPRGSVAW SDKRQRPLSQ LNRYVLHSAT
DSDADLASGD SVSLTCSISE DSLASTVTPK HQSHPGQGSV RRINGHSLLG NVNMDEEEEL
VAIARADPSK NDITLTNSED TERQGVTPGA KSIWGRQEDA SSDSRTASFF LEPLMPAVLR
PAKEKSISLN KEEESGEGRQ RGSTRRVAGA ESAASSTRRR PPQTLNRTFT PNTSSEFETT
IEPKSSEFVP PAPGQMQAFR PLVTSSVEPS SAERSPGFYL HSSVTEEKRP VQAWDAHPGT
SDIETVETIE EQDAELTKEL HPDKKQHFEE EVESAKLRED MNVKEHEDKD GGSRCSSPGQ
QSQVSSVASG SIRMTSFAER KMQRFGSNQD IRSSTSSSQR TTPDGSESCP LPLTSWRMKR
DQSPTPQNKD NANMLASELV QLHMQLEEKR RAIESQKKKM EILTARQRLK LGKAAFLHIV
KKGKSDTLPQ PTKSEFYLKE GQKLNEEKEV SSKDDTCVDA LRDRSKEAEE PEKASCEWAG
GGTVSSSPLD VEEEVDLNEC NRSIELLNEA IGSIQQQMMQ LSLQQEMLMK QNIQSPTSAT
SPLANDQINT SEPRVRASIH FVEPSGSPVV RKPPKLSSAR PRSKPSELLL GKEHSKGQKS
STPTPTDSPS ARSIQGGRTP KAESQDFVQS SVRSESFNKD KGNHKGTTFH LNDEANMRMV
SREPSSVALG VTFEESMSLR DTETTFDDGT ARDNLISSED ISRGKANLIE VDLSDLAANT
DDESTNALDV TADGSDGEKK SGMGFFFKDE QKAEDELAKK RAAFLLKQQR KAEEARLRKQ
QLEAESEQKR DETRRKAEEE RIRKEEEKAR RELIKQEYLR KKQLELCEEQ EQPQPKPKTK
PKKQRLKSVV KEEPSIDPLP KCPAANENLI SAQSGSSLSL ASVATTEPDS VNSGGAGSQR
GESVESFPGL SRNSSRTTER DWDNGSTASS ITSTSMAEYT GPKLFKEPSA KSNKPIIHNA
ISHCCLAGKV NEPQKNSILE ELERCESNHL MILFRDSGCQ FRALYSYFPD TEEIHKLTGT
GPKSITKKMI DKLYKYSSDR KQFTVIPAKT VSVSVDALTI HNHLWQAKRP AGPKKSAK
