ID G1RC65_NOMLE Unreviewed; 1573 AA.
AC G1RC65;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSNLEP00000010814.2};
GN Name=CAMSAP1 {ECO:0000313|Ensembl:ENSNLEP00000010814.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000010814.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000010814.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000010814.2}
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}.
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DR EMBL; ADFV01119747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01119755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000010814; -.
DR Ensembl; ENSNLET00000011343.2; ENSNLEP00000010814.2; ENSNLEG00000008848.3.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR InParanoid; G1RC65; -.
DR OMA; WPEVANS; -.
DR TreeFam; TF315529; -.
DR Proteomes; UP000001073; Chromosome 8.
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 CDD; cd22265; UDM1_RNF168; 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:UP000001073}.
FT DOMAIN 212..327
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1434..1568
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 353..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 866..896
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 988..1015
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 354..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1573 AA; 174613 MW; E7E11B1374BD9C31 CRC64;
MVDASGRAAA EGWRKMEAPP DGAADLVPLD RYDAARAKIA ANLQWICAKA YGRDNIPEDL
RDPFYVDQYE QEHIKPPVIK LLLSSELYCH VCSLILKGDQ VAALQGHQSV IQALSRKGIY
VMESDDTPVT ESDLSRAPIK MSAHMAMVDA LMMAYTKVVA SVKCFSMFSA LKELPYDLED
VNLKMREITE KEVKLKQQLL ESPAHQKSPS KWYWKLVPVR YRREHLSARQ SPHFPLLEDL
MRDGSDGAAL LAVIHYYCPE QMKLDDICLK EVTSMADSLY NIRLLREFSN EYLNKCFYLT
LEDMLYAPLV LKPNVMVFIA ELFWWFENVK PDFVQPRDVQ ELKDAKTVLH QKSSRPPVPI
SNATKRSFLG SPAAGTSADL QPPVQLPAEG CHRHYLHPEE PEYLGKGTAA FSPSHPLLPL
RQKQQKSIQG EDIPDQRHRS NSLTRVDGQP RGAAIAWPEK KTRPASQPTP FALHHAASCE
VDPSSGDSIS LARSISKDSL ASSIVNLTPQ NQPHPTATKT HGKSLLNNVS IEDEEEELVA
IVRADVAPQQ ADPEFPRASP RALGLTANAR SPQGQLDTSE SKPDSFFLEP LMPAVLKPAK
EKQVITKEDE RGEGRPRSIT SRKPSEGPQP LVRRKMTGSR DLNRTFTPIP CSEFPMGIDP
TETGPQSVET TGEVCGGPLA LGGFDPFPQG LSTDGFFLHV GRADEDTEGR LYVSCSKSPN
SHDSEPWTLL RQDSDSDVVD IEEAEHDFMG EAHPVVLSRY IGEEESAKLQ EDMKVKEHED
KDDASGRSSP CLSTASQMSS VSMASGSVKM TSFAERKLQR LNSCETKSST SSSQKTTPDA
SESCPVPLKT WWQKREQSPG WHGRDHAKLV QLHMQLEEKR RAIEAQKKKM EALSARQRLK
LGKAAFLHVV KKGKAEAAPP VRPEHFAKEY SQHNGEDCGD AXXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXAALLED TVGEVVDVNE CDLSIEKLNE TISTLQQAIL KISQQQEQLL
MKSPTVPVPG SKNNSQDHKV KVPVHFVEPL SPTGVAGHRK APRLGQGRNS RSGRPAELKV
PKDRPQGSSR SKTPTPSVET LPHLRPFPAS SHPRTPTDPG LDGALEPSGD PHGKCLFDSY
RLHDESNQRT LTLSSSKDAN ILSEQMSLKE VLDASVKEAG PSSSDVSGKE SVPVEEPLRS
RASLIEVDLS DLKAPDEDGE LASLDGSADL VSEGDQKPGV GFFFKDEQKA EDELAKKRAA
FLLKQQRKAE EARVRKQQLE AEVELKRDEA RRKAEEDRVR KEEEKARREL IKQEYLRRKQ
QQILEEQGLG KPKSKPKKPR PKSVHREESC SDSGTKCSST PDNLSRTQSG SSLSLASAAT
TEPESVHSGG TPSQRVESME ALPILSRNPS RSTDRDWETA SAASSLASVA EYTGPKLFKE
PSSKSNKPII HNAISHCCLA GKVNEPHKNS ILEELEKCDA NHYIILFRDA GCQFRALYCY
YPDTEEIYKL TGTGPKNITK KMIDKLYKYS SDRKQFNLIP AKTMSVSVDA LTIHNHLWQP
KRPAVPKKAQ TRK
//
