ID H0Z7P5_TAEGU Unreviewed; 1641 AA.
AC H0Z7P5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSTGUP00000006595.2};
GN Name=CAMSAP1 {ECO:0000313|Ensembl:ENSTGUP00000006595.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000006595.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000006595.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000006595.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 59729.ENSTGUP00000006595; -.
DR Ensembl; ENSTGUT00000006661.2; ENSTGUP00000006595.2; ENSTGUG00000006408.2.
DR GeneTree; ENSGT00950000182975; -.
DR TreeFam; TF315529; -.
DR Proteomes; UP000007754; Chromosome 17.
DR GO; GO:0036449; C:microtubule minus-end; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IEA:Ensembl.
DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IEA:Ensembl.
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}; Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT DOMAIN 249..364
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1502..1636
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 460..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 913..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1061..1088
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 468..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 183053 MW; 7C3159FD648D8CF6 CRC64;
MPRAAPQSPR RPPRLRGCGR RMVDVDVCAG GDSTRRKMDA LTDSAVEIVP LELYDSARAK
IAANLQWICA KAYGIDNVPE ELKDPFYIDQ YEQEHIKPPV IKLLLSSELY CRVCSLILKG
DQVAALQGHQ SVIQALSRKG IYVMESDDTP VSESDLGSAP IKMSSHMAMI DALMMAYTVE
MISIEKVVAS VKRFSTFSAS KELPYDLEDA MVFWINKVNL KMREITEKEI KLKQQLMESP
GHQKSPSKWY WKLVPVRYRR DHLSSRQLPY FPVLEDLMKD GSDGAALLAV IHYYCPEQMK
LDDICLKEVT SIADSLYNIQ LLREFSNEYL NKCFYLTLED MLYAPLVLKP NVMVFIAELF
WWFENVKPDF VQPRDIQEIK DVKAVMQQKS SRPPVPISNA TKRSFLATPA SPSPAELQPP
AQAAPEACSR YYLHPEEPDY LGKGGSPAFS PSHPLLPLRQ KQQKSLQGED SPGHRHRSNS
LTRVDGQPRG AVLAWPEKKP RPLSQPTPFA LHHSASTDVD PGSGDSISLA RSISKDSLAS
NIVNVTPKNQ PHPPSVKANG KSLLNNVEME DEDEELIAII RSEERPNRGD PEVQNAAARV
PSIVATTWSP KTNSDPSDSK PESFYLEPLM PAVLKPAKEK QVINKEDECG EGKQRSFVTK
RLNEGHLSLI RKKATSSHGE HDLNRTFTPI SSSDFTPVAD PSSADAMALG EAGVEASRPL
ASSSLDPSSQ ELSAGGFFLH AAKPDDEVTS KVSVSYGKGL SLHVQDATWT MVRHDSEPDL
LDMDDADQDL VAIDNHPIVT KYIGEEESAK LQEDMKVKEH EDKDDASGRS SPCLSTISQV
SSVSVASGSV RMTSFAERKL QRLNSYETKS STSSSQKTTP DGSESCPAPL TTWKQKREQS
PNRQNKDNVN LLASELVQLH MQLEEKRRAI EAQKKKMEAL SARQRLKLGK AAFLHVVKKG
KSPDGPQPLK PEHFAKEYSR HNGEDLDEVS LGSKSEEFLV KEEEREEMLN DSQEVAKVKM
QESLAFAEQH KPKDPAAIHD LEKSKIISVA LLEDNVTEAD INECDLSIEK LNETISTLQQ
AILKISQQQE LLMKSPTVPS PGSRNNSQDQ KVKPSIHFVE PLSPTGMNSL RKPPRLGQGR
TPRPGRPSEL KVPKDRQQNS ARVKTPTPSL ENLPHLRPFP PNSLAKTPTE VGLESSPDHG
SGSQEKCFFD TYRLHDESNQ RALVLSTSKD ANILSEMSKE MNNSFKETGL NSSDGSGKEN
VPVDEPLRSK ANLIEVDLSD LKAPDEGELE NQDSSTDMIS EGDQKSGVGF FFKDEQKAED
ELAKKRAAFL LKQQRKAEEA RLRKQQLEAE VEQKRDEARR KAEEDRIRKE EEKARRELIK
QEYLRKKQQQ ILEEQGLGKP KSKPKKPRPK SVHREESYSD SGTKCSSTPD NLSSAQSGSS
LSLASAATTE PESVHSGGTP SQRVESMESL PILSRNPSRN TERDWENAST ASSIASVAEY
TGPKLFKEPS SKSNKPIIHN AISHCCLAGK VNEPHKNSIL EELEKCDANH YIILFRDAGC
QFRALYCYYP DTEEIYKLTG TGPKSITKKM IDKLYKYSSD RKQFNVIPAK TMSVSVDALT
IHNHLWQAKR PAVPKKSQTR K
//
