ID A0A1S3ACP3_ERIEU Unreviewed; 1253 AA.
AC A0A1S3ACP3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 3 {ECO:0000313|RefSeq:XP_007532901.1};
GN Name=CAMSAP3 {ECO:0000313|RefSeq:XP_007532901.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007532901.1};
RN [1] {ECO:0000313|RefSeq:XP_007532901.1}
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_007532901.1; XM_007532839.2.
DR AlphaFoldDB; A0A1S3ACP3; -.
DR GeneID; 103122249; -.
DR CTD; 57662; -.
DR eggNOG; KOG3654; Eukaryota.
DR InParanoid; A0A1S3ACP3; -.
DR OrthoDB; 2918432at2759; -.
DR Proteomes; UP000079721; 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:UP000079721}.
FT DOMAIN 228..339
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1113..1247
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 183..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..760
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..878
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 135234 MW; B44C29E15246544B CRC64;
MVEAAPPGPG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE HVPSELWEPF
YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLETPPS PSALLALLAR RGTVPALPER
PVQEADLRHQ PILMGAHLAV IDALMVAFAF EWTKTLPGPL ALASLEHKLL FWVDTTIRRL
QEKTEQEATQ RASPAAPADG VAPAQPSCPT RWYWKLVPHA IAFCLKESGS KPPMIRYRKD
RAVARRAPCF PAVTSLQDLA SGAALAATIH CYCPQLLRLE EVCLKDPMSV ADSLYNLQLV
QDFCASRLPR GCPLALEDLL YVPPPLKINL VVLLAEMFMC FEVLKPDFVQ AKDLPDGHAA
SPRAAETATP QNSGSSSPVF NFRHPLLSSG GPQSPLRGST GSMKSSPSMS HMEALGKAWN
RQLSRPLSQA ASFSTPFGLD SDVDVVMGDP VLLRSVSSDS LGPPRPAAAA AAASPGPPPP
TAEPGELPTI EEALQIIHSA EPRLLPDGAA DGSFYLHSPE GPNKAPVYLS HPEPPLKPEP
PGPPAGQAQP SEGSSSPKAQ PSEVKMTSFA ERKKQLVKPE TDPGSLAAVA ATGGLPPEAL
SSEMSELGAR LEEKRRAIEA QKRRIEAIFA KHRQRLGKSA FLQVQPREAS GETEAEPEAE
AEPSPVPGGE RAAGEGQGEP SPRPKVVTFS ADVGPPPPEG LGDYNKAVSK LSAALNSLQR
DMQRLTDQQQ RLLAPPDPPG PAPASATWVI PGPPSAPKAA SPSPARRAPA SRRSPGPSPA
PRSPKHTRPA ELRLAPLTRV LTPPHDVDSL PHLRKFSPSQ VPVQTRSSIL LTQGTPPEEP
PSRPGLIEIP LGSLEEPPAE DEADGSPPGA EDSLEEEASS EGEPRAGLGF FYKDEDKPED
EMAQKRASLL ERQQRRAEEA RRRRQWQEAE KEQRREEAVR LAQEDVAPTP PAPAAPQAPP
TGAPAGRGPA EEEVGPRRGD FTRLEYERRA QLKLMDDLDK VLRPRAVGTG GPSRGGRRGP
RPRSGCCDDS ALARSPARGL LGSRLSKVYS HSTLSLSTVA NEAPNNLGVK GPMSRAPSPS
GLMSPSRLPG SRERDWENGS NASSPASVPE YTGPRLYKEP SAKSNKFIIH NALSHCCLAG
KVNEPQKNRI LEEIEKSKAN HFLILFRDSS CQFRALYTLS GDTDELCRLT GYGPRTVTPA
MVEGIYKYNS DRKRFTQIPA KTMSMSVDAF TIQGHLWQNR KPTTPKKGGG IPK
//
