ID F1MYW2_BOVIN Unreviewed; 1576 AA.
AC F1MYW2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSBTAP00000007892.5};
GN Name=CAMSAP1 {ECO:0000313|Ensembl:ENSBTAP00000007892.5,
GN ECO:0000313|VGNC:VGNC:26730};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000007892.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000007892.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007892.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000007892.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007892.5};
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 RefSeq; NP_001179025.1; NM_001192096.1.
DR SMR; F1MYW2; -.
DR STRING; 9913.ENSBTAP00000007892; -.
DR iPTMnet; F1MYW2; -.
DR PaxDb; 9913-ENSBTAP00000007892; -.
DR Ensembl; ENSBTAT00000007892.6; ENSBTAP00000007892.5; ENSBTAG00000006008.6.
DR GeneID; 506553; -.
DR KEGG; bta:506553; -.
DR CTD; 157922; -.
DR VEuPathDB; HostDB:ENSBTAG00000006008; -.
DR VGNC; VGNC:26730; CAMSAP1.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; F1MYW2; -.
DR OMA; EANHYII; -.
DR TreeFam; TF315529; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000006008; Expressed in retina and 102 other cell types or tissues.
DR ExpressionAtlas; F1MYW2; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
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; 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:UP000009136}.
FT DOMAIN 216..331
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1437..1571
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 348..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 865..895
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 358..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 172740 MW; 54873366E08CAC2E CRC64;
MVDAGGCPAG EGWRRMEAAP DGAVDIVPLD RYDPARAKIA ANLQWICAKA YGRDDIPEDL
RDPFYIDQYE QEHIKPPVIK LLLSSELYCR VCSLILKGDQ VASLQGHQSV IQALSRKGIY
VMESDDTPVT EPDLSHAPIK MSAHMAMVDA LMMAYTVEMI SIEKVVASVK RFSTFSASKE
LPYDLEDAMV FWVNKVNLKM REITEKEVKL KQQLLESPAH QKVRYRREQL CARQPPHFPL
LEDLMRDGSH GAALLAVVHY YCPGQLKLDD ICLKEVTSMA DSLYNIRLLR EFSNEYLNKC
FYLTLEDMLY APLVLKPNVM VFIAELFWWF ENVKPDFVQP RDVQELKDAK SVSYPKSSRP
PVPISNATKR SFLGSPAAAS PADLQLGEPE PPPAAGDFSL PSSLFRGKGA SAFSPSHPLL
PLRQKQQKTV QGEDPPDQRH RSNSLTRADS QPRGAAIAWT EKKNRPVSQP APFALHHTAS
CDMDPGGGDS VSLARSISKD SLASSVVHLT PQNQPQPAAL RTDGRSLLSN VDIEDEDEEL
LAIVRTDVAR QGGDPGPMAG ARSPHRLADA FESKTDSFFL EPLMPAVLRP AKEKQVVTKE
DECGEGRPRA FTSRRSGDGH QPLGRKKAPS SHVARDLNRT FSPISCSEMS AGFEAVPAEV
GPQVAGDTHG GSLAGSSFDP SSQGQSADGF FLHVGRADKD AEGRLYMSCA RSPGALSPDT
WAVLRQDSDS DVADLDEAEQ DFAGEEHPAV RAGYGGEEES AKLQEDLKVK EHDDKDDASG
RSSPCLSTVS QTSSASMASG SAKMTSFAER KLQRLNSCET KSSASSSQKT TPDASESCPA
PLTTWKQRRE QSPSRPGGDH ASLLASELLQ LHMQLEEKRR AIEAQKKKVE ALSARQRLQL
GKAAFLHVVK KGRADATQQP LKVGSLAGEH AQHNGDDFLG KEEGRGALLG SPDVDGEGLA
LVQPHKARDP ASLPELEHGK ALSAVLLEDT EGVDVGECDL SIEKLNETIS TLQQAILRIS
QQQEQLLLKS PTLPSPGPRN GAQDPKAKAA IHFVEPLSPT ALTGHRKPPR LGQGRNARSG
RPAELKVPKE RQQGSSRSKT PTPGLETAPH SRSFPPRTPP EPGWDGPSEP GSEASEKCVF
DSYRLHDESN QRTLVLSSSR DANVLSEQGG FREGLEGSAK EAGLSTLPAP GKENVPLDEP
PRSKASLIEV DLSDLKAPDE DGETEGRDSS VDLGSEGDQK PGVGFFFKDE QKADDELAKK
RAAFLLKQQR KAEEARVRRQ QLEAEVELKR DEARRKAEED RIRKEEEKAR RELIKQEYLR
RKQQQILEEQ GLGKPKTRPR KPRPKSVHRE EPGSDLGPKS ASPPDNLSRA QSGSSLSLAS
AATTEPESVH SGGTPSQRVE SLEALPVLSR NPSRSTDRDW ETASAASSLA SVAEYTGPKL
FKEPSSKSNK PIIHNAISHC CLAGKVNEPH KNSILEELEK CDANHYIILF RDAGCQFRAL
YCYYPDTEEI CKLTGTGPKS IAKKMIDKLY KYSSDRKQFS LIPAKTMSVS VDALTIHNHL
WQPKRPSAPK KTQTRK
//
