ID A0A3Q0R9Z7_AMPCI Unreviewed; 1244 AA.
AC A0A3Q0R9Z7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Calmodulin regulated spectrin-associated protein family, member 3 {ECO:0000313|Ensembl:ENSACIP00000008944.1};
GN Name=CAMSAP3 {ECO:0000313|Ensembl:ENSACIP00000008944.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000008944.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000008944.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 61819.ENSACIP00000008944; -.
DR Ensembl; ENSACIT00000009215.1; ENSACIP00000008944.1; ENSACIG00000006919.1.
DR GeneTree; ENSGT00950000182975; -.
DR OMA; SPQMTTW; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0016020; C:membrane; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW ProRule:PRU00841}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 309..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..296
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1106..1244
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 448..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 138200 MW; 7FC4B209AD8555CF CRC64;
MVDSPTMRKT FVVPDIKPLD LYDCTKSKIC ASVGWLLAKS YGSTENVPAE LRDPFYCDQY
EQEHLKPPVT RLLQSSELYC RTYSILQGGT ATEAQPKDNV TLLQLLTRRG IVAKDQDTAV
TDADLRHKPI KMSAHLAVID ALMAVGAMET VTAVKTCGSA ELLGKAASWE DALLHWVNEV
RSKPEKNNLR YRKDKIQSKL KPTFPVVNEV KDLSSGCAVA AVIHYYCPGL LRLEDVCMKD
SMCVADSLYN LQFIREFCDS CLKSCCHLAL EDMLYTPQEL QINLLSFLSE LLSWFEVQRP
EFVQPIDTLI LFSCLGGYLF GWVFEIFVNV FPFILCVWFV CIPVFACLYM SAYVPLYSGS
LTQSTSMSHI EGAGKTWSKK PLSRPLSAVS FSIPFGLDSD VDIVMGNPVI TRSVSSDQLN
PAGQTMARVP YTPPEDLKLP TIEEALQIIH NESKMEPRLH PDGAPDGFYL HSPDDPASSR
YNSNLAPISC SAPTRSGMMY RPTGESSEPI RTRNTSECSR DDDSVLRDGS VDSDASEDLP
KAHSTPSTPA AAAVRGGKEV PDSGVKMTSF AERKKRQITD SPKSSDLSSP QMTTWAQKSE
ESPSKSPQLN NEMSELGVRL EEKRKAIEAQ KKRIEAIFAK HRQRLGKSAF LQLKKEQXED
EGEGNGEDVE DEGTVKRGLG LNKQVIQSKE KAGTPGEKYH GTPAEKMVAP LGDYNNAVSK
LTAALSSLQS DMQRLTEQQN HPKTSTSAPP PARLSRETTR DLNSASSSPS PSRKMANHTN
PPKSPHVHRR AQSVPPKSPK HSRPSDAKVP ILSRVLTPPQ NVDRIPHLRR VNPWQSQVQT
SSSFSIGDSG SLDELRPAAE DALLIEISLS ALGGGGEEDD DQLPDAFSDS SDRTEAENKA
GLGFFFKDDK DRPEDEMAQR RAALLEKQQK RTEEMKRRKL EQEKEKELNE DRPQTPGTPP
SSQTPPADGT PQRRGDFTKQ EYERRQQLKI MEDLDKVLRQ KPTTVRGVKK QRPKTMFRDD
SVLSQSPVKG FMGTKLNKVY SHSSVNLSSM ANDSGGMTVR KSPSRSHSPA RSRGRSPGRI
GPQNGEKDWE TGSTISSPAS IPEYTGPKLY KEPSFKSNKF IIHNAITRCC LAGKVNEPQK
NKIVEEMEKS AANHFLILFR DSSCQFRAVY TMNPETDEMV RLTGIGPRVI TLDMVESIYK
YSSDRKQFTV IPSKTMSMSV DAFTIPGCFW QKRPGTPKKL GTPK
//
