ID A0A2U3WSB7_ODORO Unreviewed; 1271 AA.
AC A0A2U3WSB7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 3 isoform X1 {ECO:0000313|RefSeq:XP_004412228.1};
GN Name=CAMSAP3 {ECO:0000313|RefSeq:XP_004412228.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004412228.1};
RN [1] {ECO:0000313|RefSeq:XP_004412228.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_004412228.1; XM_004412171.1.
DR AlphaFoldDB; A0A2U3WSB7; -.
DR STRING; 9708.A0A2U3WSB7; -.
DR GeneID; 101386830; -.
DR KEGG; oro:101386830; -.
DR CTD; 57662; -.
DR InParanoid; A0A2U3WSB7; -.
DR OrthoDB; 2918432at2759; -.
DR Proteomes; UP000245340; 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};
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:UP000245340}.
FT DOMAIN 228..339
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1131..1265
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 357..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..895
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 136823 MW; 9B4B062E76974AD5 CRC64;
MVEAAPPGPG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE HVPSELWEPF
YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLETPPN PSALLALLAR RGTVPALPER
PVQEADLKHQ PILMGAHLAV IDALMVAFAF EWTKTLPGPL ALASLEHKLL FWVDTTIRRL
QEKTEQEAAQ RASPVAPADG VAPAQPSCPT RWYWKLVPHA IAFCLKESGS KPPMIRYRKD
RAVARRAPCF PNVTTLQDLA SGAALAATIH CYCPQLLRLE EVCLKDPMSV ADSLYNLQLV
QDFCASRLPR GCPLSLEDLL YVPPPLKINL VVLLAEMFMC FEVLKPDFVQ AKDLPDGHAA
SPRATEASPA QNSSGCSSPV FNFRHPLLSS GGPQSPLRGS TGSLKSSPSM SHMEALGKAW
NRQLSRPLSQ AVSFSTPFGL DSDVDVVMGD PVLLRSVSSD SLGPPRPVPA RTPVQPPPEP
GDLPTIEEAL QIIHSAEPRL LPDGAADGSF YLHSPEGSSK LPLASSYPLD GASKPLPAVP
TQAPSYVPHP EGPLKPSPCP AGELSKSPAL SEGSPKAAAS SPAAGNSEVK MTSFAERKKQ
LVKAEAEAGS PAATPAAAEA LSSEMSELGA RLEEKRRAIE AQKRRIEAIF AKHRQRLGKS
AFLQVQPREA GGEAEADPGP VPGGERPAGE GQGDPAPRPK AVTFSPELGP VPPEGLGDYN
RAVSKLSAAL SSLQRDMQRL TDQQQRLLAP PEAPGPAPPP AAWVIPGPTV GPKAASPSPA
RRAPAARRSP GPGPSPTPRS PKHARPAELR LAPLTRVLTP PHDVDSLPHL RKFSPSQVPV
QTRSSILLAE GSPPEEPVAR PGLIEIPLGS LEEPTAEDEG DGSPPGAEDS LEEEASSEGE
PRAGLGFFYK DEDKPEDEMA QKRASLLERQ QRRAEEARRR KQWQEAEKEQ RREEAARLAQ
EVVTAGAPAP PAPVAPTAAP APAGRAPPEE EVGPRRGDFT RLEYERRAQL KLMDDLDKVL
RPRAVGTGGP GRGGRRAPRP RSGCCDDSAL ARSPARGLLG SRLSKVYSQS TLSLSTVANE
APNNLGVKRP TSRAPSPSGL MSPSRLPGSR ERDWENGSNA SSPASVPEYT GPRLYKEPSA
KSNKFIIHNA LSHCCLAGKV NEPQKNRILE EIEKSKANHF LILFRDSSCQ FRALYTLSGE
TEELTRLAGY GPRTVTPAMV EGIYKYNSDR KRFTQIPAKT MSMSVDAFTI QGHLWQSKKP
TTPKKGSSTP K
//
