ID A0A3P8U4C5_AMPPE Unreviewed; 1582 AA.
AC A0A3P8U4C5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Calmodulin regulated spectrin-associated protein 1a {ECO:0000313|Ensembl:ENSAPEP00000030147.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000030147.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000030147.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000030147.1}
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 STRING; 161767.ENSAPEP00000030147; -.
DR Ensembl; ENSAPET00000030952.1; ENSAPEP00000030147.1; ENSAPEG00000021431.1.
DR GeneTree; ENSGT00950000182975; -.
DR Proteomes; UP000265080; Chromosome 16.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR CDD; cd22265; UDM1_RNF168; 1.
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};
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:UP000265080}.
FT DOMAIN 248..363
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1447..1581
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 175708 MW; 34CE1DB18918BD65 CRC64;
MDVEVSAGRD STWRRAAAAA DDDGGGGGGG GGGVEAQVVP LELYDSARAK IEANLRWLFA
KAYGIDDIPA DLRDPFYTDQ YEQEHIKPPI IRLLLSGELY CRVCGLILHA EQAASLQSHQ
SVIQNLSRKG IYVLEADNTP VSDLDLSSFP IKMNSHIHLI DALIMAYTVE MISIEKVVSS
VKRFSNFSAS KELPFDLEDA MVFWINKVNI KMREITEKEC KMKQHLLESP SHQKPDIMHA
LAHCLLEPVE FSRVVRYRRD HLSGRTLQHF PLLDDLFKDV CDGTALLAVI HFYCPELIRL
EDICLKDVPS IADSVYNIQL LREFSNEYLN KCFYLNPEDL LYSPPVLKNN VMVFIAELFW
WFENVKPDFV QPRDLQEVKD VRLLLQPKSS RSYVPISNVT KRSFLTSSSS ADVLTTPLSP
DLSTKQSSTS PSHSLLPLRQ RQQKVTEESS SDVRNRSNSL TRTEGQHQGS ILAWPERRAR
PLSQPAPYAL HFAQEDDADS ISLARSISKD SLASNIMSIT PKHMLGSGLS QHRLSGQSLL
SHMRIEDEEE EIEEEELVAV IHPSAFSRKR IGSDMEQDEL EIQSAASTSR VPKTSCSPRL
DTGPFTLDHQ ADSYFLEPLI PAIPKPAKEK SISLNKQEES GESRFRPVAG ARKAAINVPS
ASQRKSPMAE SNRSICTPTL MVESVPTSLR PPTEGSAGIS QSGKKQSQGF FLHLSGESDC
HSPFSTGLEA GHDSDSDIAD LEEDDDDDDQ MELTKEVVKR GRGRFLEEGD LTEFGEGEGE
SAKLREDSKV SERDDKEDGS GRSSPCPSTI SWASSCSASG SASVKMTSFA ERKLLKLGLR
DGYSSTSSSQ KTTPDGSEVA PCPPWQLRSE PTSGWLGKEP STVLGKNMMA SPPVVPSELL
QLHMQLEEQR RAIEYQKKKM ETLSARQRLK LGKAAFLNIV KKGGGRSDTL PLPLKHPQES
TELTAADRSK SKTHSCRDDS CLDALKVQAR AGQTEGGQVN RDNKLNPMSQ DNGAEPDLNE
CSRSIDLLNE AISSIQQQMM HLSLQQDLLM KQSVVSPPDS VQSDPSTNPN TALTELSTSD
SRSYAVHFVD ISGRNPVPAR RPPKLSSSQR RKASERKQSK EHSRAASVKL NVPSPDCILS
AETGSIIESS RTDKSVQRST TFRVRDGSGE GTGRCSDKPQ SQDPPVISNA SNSDSQDAEQ
EIKAVISGKE FVGGDESTRV KGQLIEVDLS EVKDRLEDGS TDATDGMAEG EQKNVLGFFF
KDDEKAEDEM AKRRAAFLLK QQRKAEEARL RKQQQEAESE IKRDEARRKA EEDRIRKEEE
KARRELIKQE YLRRKQQALM EEQGLVKPRP RTKSRRNRPK SLHREESNSL SKGSTTPDLS
CSHRGSTLSL ATEVDSVISG GAESHRAGSV CSMESFPLLS RASSRNMERD WENGSIASSI
TSTEYNGPKL FKEPSSKSNK PIIINAIAHC CLAGKVNEAQ KNVVLEELEK CESNHLIILF
RDGGCQFRAI YSYSPDTEEI VKFTGTGPRH ISRKMIDKLY KYSSDRKQFT VIPAKTVSVS
VDALTIHNHL WQVKRPGSAR RK
//
