ID U3JGF5_FICAL Unreviewed; 1675 AA.
AC U3JGF5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSFALP00000001859.2};
GN Name=CAMSAP1 {ECO:0000313|Ensembl:ENSFALP00000001859.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001859.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000001859.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000001859.2}
RP IDENTIFICATION.
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 RefSeq; XP_005055734.1; XM_005055677.2.
DR STRING; 59894.ENSFALP00000001859; -.
DR Ensembl; ENSFALT00000001869.2; ENSFALP00000001859.2; ENSFALG00000001788.2.
DR GeneID; 101817885; -.
DR CTD; 157922; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR OrthoDB; 2918432at2759; -.
DR Proteomes; UP000016665; 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:UP000016665}.
FT DOMAIN 283..398
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1536..1670
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 947..977
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1095..1122
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1675 AA; 185987 MW; D5F58BC6A3263E81 CRC64;
MSLGRSAASR GCRGDGSDAG ERSAPSPPAL SPPALSPGLP WAPMPRGAAQ SPRRPPRLRG
CGGRPAMVDV DVCAGGDSTR RKMDALTDSA VEIVPLELYD SARAKIAANL QWICAKAYGI
DNVPEELKDP FYIDQYEQEH IKPPVIKLLL SSELYCRVCS LILKGDQVAA LQGHQSVIQA
LSRKGIYVME SDDTPVSESE LGSAPIKMSS HMAMIDALMM AYTVEMISIE KVVASVKRFS
TFSASKELPY DLEDAMVFWI NKVNLKMREI TEKEIKLKQQ LMESPGHQKV RYRREHLSSR
QLPYFPVLED LMKDGSDGAA LLAVIHYYCP EQMKLDDICL KEVTSIADSL YNIQLLREFS
NEYLNKCFYL TLEDMLYAPL VLKPNVMVFI AELFWWFENV KPDFVQPRDI QEIKDVKAAM
QQKSSRPPVP ISNATKRSFL ATPASPSPAE LQPPAQAAPE ACSRYYLHPE EPDYLGKGGS
PAFSPSHPLL PLRQKQQKSL QEEDSPGHRH RSNSLTRVDG QPRGAVLAWP ERKPRPLSQP
TPFALHHSAS TDVDPGSGDN ISLARSISKD SLASNIVNVT PKNQPHPASV KANGKSLLNN
VEMEDEDEEL IAIIRSEERP SRGDPEVQSA AARVPSIVAT AWSPKTNSDP SDSKPESFYL
EPLMPAVLKP AKEKQVINKE DECGEGKQRS FVTKRLNEGH LSLLRKKATS SHGEHDLNRT
FTPISSSDFT PVADPTSADA VALGEAGVEA SRPLASSSLD PSSQELSTGG FFLHAAKPDD
EVTSKGNVSY GKGLNLHVQD TTWTMVRQDS EPDLLDMEDA DQDLVVIDNH PIVTKYIGEE
ESAKLQEDMK VKEHEDKDDA SGRSSPCLST ISQVSSVSMA SGSVRMTSFA ERKLQRLNSY
ETKSSTSSSQ KTTPDGSESC PAPLTTWKQK REQSPNRQNK DNVNLLASEL VQLHMQLEEK
RRAIEAQKKK MEALSARQRL KLGKAAFLHV VKKGKSPDGP QPLKPEHFGK EYSRHNGEDL
DEVSLGSKSE EFLVKEEERE EMLNDSQEVA KVKMQESLAF AEQHKPKDPT AIHDLEKSKI
ISVALLEDNV TEADINECDL SIEKLNETIS TLQQAILKIS QQQELLMKSP TVPSPGTRSN
SQDQKVKPSI HFVEPLSPTG MNSLRKPPRL GQGRTPRPGR PSELKVPKDR QQNSARVKTP
TPSLENLPHL RPFPPNSLAK TPTEVGLESS PDHGSGSQEK CFFDTYRLHD ESNQRALVLS
TSKDANILSE MSKEVNNSFK ETGLNSSDGS GKENVPVDEP LRSKANLIEV DLSDLKAPDE
GELDNQDSTT DMISEGDQKS GVGFFFKDEQ KAEDELAKKR AAFLLKQQRK AEEARLRKQQ
LEAEVEQKRD EARRKAEEDR IRKEEEKARR ELIKQEYLRK KQQQILEEQG LGKPKSKPKK
PRPKSVHREE SYSDSGTKCS STPDNLSSAQ SGSSLSLASA ATTEPESVHS GGTPSQRVES
MESLPILSRN PSRNTERDWE NASTASSIAS VAEYTGPKLF KEPSSKSNKP IIHNAISHCC
LAGKVNEPHK NSILEELEKC DANHYIILFR DAGCQFRALY CYYPDTEEIY KLTGTGPKSI
TKKMIDKLYK YSSDRKQFNV IPAKTMSVSV DALTIHNHLW QAKRPAVPKK SQTRK
//
