ID A0A3Q3GCU9_9LABR Unreviewed; 1437 AA.
AC A0A3Q3GCU9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Calmodulin regulated spectrin associated protein family member 3 {ECO:0000313|Ensembl:ENSLBEP00000028803.1};
GN Name=CAMSAP3 {ECO:0000313|Ensembl:ENSLBEP00000028803.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000028803.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000028803.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; ENSLBET00000030153.1; ENSLBEP00000028803.1; ENSLBEG00000021792.1.
DR GeneTree; ENSGT00950000182975; -.
DR Proteomes; UP000261660; 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 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:SF2; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 3; 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:UP000261660}.
FT DOMAIN 202..316
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1299..1437
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 419..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 174..201
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 520..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 158157 MW; 73516D8BD09827E3 CRC64;
MVDSPTMRKT FVVPDIKPLD LYDCTKAKIC ASVGWLLAKS YGSAENVPAE LRDPFYCDQY
EQEHLKPPVT RLLQSSELYC RTYSLIQGGT GAEAQPKDNA ALVQLLTQRG LLSKEQDVPV
TDADLRHKPI KMSAHLAVID ALMAAGAMET VTAVKSCASA KLLGGAASWE DALLNWVNEL
NQKLRERAEA AQNDSSQALT EPQPVQPSLR YRKDKIQSKQ KPIFPAVNEV KDLSTGCAVA
AVIHYYCPGL LRLEDVCMKE TMSAADSLYN LQFIKEFCDS CLRSCCHLAM EDMLYVPREL
QLNLLSFLAE LLNWFEVQRP EFVQPIDTLC GATAGAQRNP SGNSTSPSIF KKPFLPISSP
ASGSLTQSTS MSHIEGVGKT WGKKPLSRPL SAVSFSIPFG LDSDVDIVMG NPVITRSVSS
DQLNPAGQNM TRVPFTPPED LSHLLSKPPG PNGPQRASWA TQTPSIPRMA EENGLPASET
GELPTIEEAL QIIHNESKME PRLHPDGAPD GFYLHSPDDP ASSRHNNNLA PISCSAPTRS
GMMYRPTGES REPTRTRNTS ECSRDDDSVL RDGSVDSDAS EDLPKVQSMP STPAAGSQSA
SGNGKETSDS GVKMTSFAER KKKQILDSPK ASDPSSPSMT TWTQKSEESQ NKSPQLNNEM
SELGVRLEEK RKAIEAQKKR IEAIFAKHRQ RLGKSAFLQL KKEQNEEEGG GDGQTSTSST
EEDLSRLTLE ERLARMEEED QQEPDEKHCS VDDDGTVRGG PLSHSKEKAG TPGDKGSGTP
GEKMVAPLGD YNNAVSKLTA ALSSLQSDMQ RLTEQQNQLV KKKAADSSNN SWVIPASPKT
STPAPSHARA SRESTRDLNS ASSSPSPSRK ITNHTTPHKS PRVQRRAQSV PPKSPKHNQH
NRPLDLKTPT LSRVLNTSQN VDRIPHLRRV NPWQSQVQTS SSFSIGDSDS LDDLRSSGLT
PLTTPTPTPR PAADDVLSEV GSNDDQSIFS MDLESGPSHG HLARKEDLPG GGCSSGAASE
CSFESDAPAV VSNGKHSSLI EISLSSLRGD REEDDQVPDV FSNSMTDGTE QDLKGGVGFF
FKDDKERPED EMAQRRAALL EKQQKRAEEL KRRKLEQEKE KEKEKEKESN KPQWMVIEGW
GNKGEDRPQT PGTPPASSPQ PSEGTPQRRG DFTRQEYERR HQLKIMEDLD KVLRQKPTTV
RGVKKQRPKT VFRDDSVLSH SPAKGFMGTR LNKVYSHSTL NLSSMANDSG GLTVRKSPSR
SHSPSRLMSP RRMSAQNGER DWENGSTISS PASIPEYTGP KLYKEPSFKS NKFIIHNAIT
RCCLAGKVNE PQKNKIVEEM EKSAANHFLI LFRDVSCQFR AVYTMNPETE EMVRLTGIGP
RIIAPEMVES IYKYSSDRKQ FTVIPSKTMS MSVDAFTIPG HFWQKRPGTP KKLGTPK
//
