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Database: UniProt
Entry: A0A3Q1CVQ2_AMPOC
LinkDB: A0A3Q1CVQ2_AMPOC
Original site: A0A3Q1CVQ2_AMPOC 
ID   A0A3Q1CVQ2_AMPOC        Unreviewed;      1562 AA.
AC   A0A3Q1CVQ2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 1-B-like {ECO:0000313|Ensembl:ENSAOCP00000029634.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029634.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000029634.1}
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   Ensembl; ENSAOCT00000023937.1; ENSAOCP00000029634.1; ENSAOCG00000020074.1.
DR   GeneTree; ENSGT00950000182975; -.
DR   OMA; FIAEVFW; -.
DR   Proteomes; UP000257160; Unplaced.
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:UP000257160}.
FT   DOMAIN          228..343
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1427..1561
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          391..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          972..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1129..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1269..1296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1318..1364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..731
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1348..1364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1562 AA;  173490 MW;  1D52AF6D35EA38D1 CRC64;
     MDVEVSAGRD STWRRAAADD DGGGGGGGGG GGGVEAQVVP LELYDSARAK IEANLRWLFA
     KAYGIDDIPA DLRDPFYTDQ YEQEHIKPPI IRLLLSGELY CRVCGLILHA EQAASLQSHQ
     SVIQNLSRKG IYVLEADNTP VSDLDLSSFP IKMNSHIHLI DALIMAYTVE MISIEKVVSS
     VKRFSNFSAS KELPFDLEDA MVFWINKVNI KMREITEKEC KMKQHLLESP SHQKVRYRRD
     HLSGRTLQHF PLLDDLFKDV CDGTALLAVI HFYCPDLIRL EDICLKEVPS 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 AELTAADRSK SKTHSCRDDS
     CLDALKVQAR AGQTEGGQVN RDNKLNPMSQ DNGAEPDLNE CSRSIDLLNE AISSIQQQMM
     HLSLQQDLLM KQSVVSPPDS VQSDPSTNPN TAQTELSTSD SRSYAVHFVD ISGRNPVPAR
     RPPKLSSSQR SKASERKQSK EHSRAALVKL NVPSPDCILS AETGSIIESS RTDKSVQRST
     TFRVRDGIGE GTRRCSDKPQ SQDPPVISNA SNSDSQDAEQ EIKAVISGKE FVGGDDSTRV
     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 CLAGKVNESQ KNVVLEELEK CESNHLIILF RDGGCQFRAI YSYSPDTEEI
     VKFTGTGPRH ISRKMIDKLY KYSSDRKQFT VIPAKTVSVS VDALTIHNHL WQVKRPGSAR
     RK
//
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