ID A0A2D0PVF0_ICTPU Unreviewed; 1363 AA.
AC A0A2D0PVF0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 3 isoform X5 {ECO:0000313|RefSeq:XP_017310019.1};
GN Name=camsap3 {ECO:0000313|RefSeq:XP_017310019.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017310019.1};
RN [1] {ECO:0000313|RefSeq:XP_017310019.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017310019.1};
RG RefSeq;
RL Submitted (SEP-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 RefSeq; XP_017310019.1; XM_017454530.3.
DR Ensembl; ENSIPUT00000008958; ENSIPUP00000008587; ENSIPUG00000005870.
DR GeneID; 108257105; -.
DR CTD; 57662; -.
DR OMA; GASKWED; -.
DR OrthoDB; 2918432at2759; -.
DR Proteomes; UP000221080; Chromosome 24.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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: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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW ProRule:PRU00841}.
FT DOMAIN 165..285
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1224..1358
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 297..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1086
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 149898 MW; 5FB61D7E929A528F CRC64;
MVDSNAMRKT FVVPDVKPLD QYDINRAKIC ASVGWLLAKS YGNADSVPAE LRDPFYLDQY
EQEHLKPPVT RLLQSPELYC RTYGLLLAGG PGANGTPTDN TVLLQTLSKK GLTPRDQNTP
VTEADLRHKP IKMSAHLAVM DALMAVGAME TVRASGGVER LGGEDDWERT LLHWVNTLRY
RKDKLLSKLK PCFPVVNEVK DLSNGCAIAA VIHYYCPGLL RLEDVCMKES MSLADSLYNL
QLILEFCESC LKSCCPLVLE DMLYSPPELQ VNMLSFLAEL LYWFEVSKPD FVQPLNATES
SGGSENGNRG SGSSSPSLFK KPFLPISPAT PIPGSLTQST SMSHVEAAGR SWTKNPLSRP
LSSAVSFSIP FGLDSDVDIV MGNPVIMRSV SSDNINPAGQ PGKRAHYTPP EDISRSPGPN
GPQRASWASR SPAVPLLAEE NGLDEGDAAE LPTIEEALQI IHNEGKMEPR LHPDGAPDGF
YLHSPDDPAS RRHNGSPAIL GGSAPSGAGM QYRPMGNASC TRRTSDGSRD DDSVLRDGSV
DSDASEDLPK TQSTPATPAG GARVANSSGQ ETPDSGVKMT SFAERKKKLA QEQPIPDEDP
QMTSWAAKKT QESPSKSPAL TSEMSELGAR LEEKRKAIEA QKRRIEAIFA KHRQRLGKSA
FLQLKKEQEE DVEGVSAEED VRRMSLDERL ARMEKDEESD AKQEKERPPD DRKFQTSAQQ
ASKDKTVAGP SGEKTGVPLG DYNNAVSKLN AALSSLQNDV QRLSEQQNQL LLKKIPSANQ
TWVIPPSTKS SAAAAPPRLS RESTRDLIPN SSSSSPSPSR RISSQAIPPK SPGSHRRAQS
APPKSPKNQH HSRSADPKMP TLTRVITAPH CVDSMPHRRK VSPWHYRDQT SSSFSFGSSV
SQSDSRPPSR PLSEDTSDDQ TVFSLELDGG SNHFPGRREH HGGSSSGAPS ECSFESDIPA
SAFTRKPSSL IEIPLSSLSG LDREDAEHGL DAASDSMSDH TEPETKTGIG FFFKQDEARP
EDEMAQRRAA LLEKQQKRAE EIKRKRQEQE REKEASRRNS VDELERPRTP STPPPARTPP
AAHTPPPDGS QHRRGTFTRQ EYEWRHQLKI MEDLDKALRQ KPTTVRGVKK QRPKTVFRDD
SDLSRSPAKG LLGSRLNKVY SHSTMNLSSM ANDTGTLTIK KSPSRSHSPS RLMSPGRMAT
QNGDKDWENA STLSSPASIP EYTGPKLYKE PSFKSNKFII HNAISRCCLA GKVNEPQKNK
IIEEMEKSSA NHFLILFRDS SCQFRAVYTM NPETEELVRL TGIGPRIISL SMVESIYKYS
SDRKQFSVIP SKTMSMSVDA FTIPGQLWQT KRPGTPKKLG TPK
//