ID A0A3B4GSQ6_9CICH Unreviewed; 1350 AA.
AC A0A3B4GSQ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Calmodulin regulated spectrin associated protein family member 2 {ECO:0000313|Ensembl:ENSPNYP00000026237.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000026237.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000026237.1}
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; 303518.ENSPNYP00000026237; -.
DR Ensembl; ENSPNYT00000026876.1; ENSPNYP00000026237.1; ENSPNYG00000019756.1.
DR GeneTree; ENSGT00950000182975; -.
DR Proteomes; UP000261460; 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 CDD; cd22265; UDM1_RNF168; 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:SF1; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 2; 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}.
FT DOMAIN 211..324
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1210..1344
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 197..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 666..696
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 783..820
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 587..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 150156 MW; 6159635F94DF211F CRC64;
MGEVQDVRDV KKTFVAPAIK SFEHYDFSRA KMCCSLTWLV AKAYGTDSIP ADLKDPFYTD
QYEQEHLKPP VASLLLSADL YCRAGSLILK SDAAKPLLGH DAVIQALAQR GLYVTDQERL
VTERDLRKRP LQMSAHLAMI DTLMMAYTVE AVSVEKVMAC ICQYPSCYPE VETPYDTEDA
VTTWINKVNE YLKETVAQEQ RKKETQGTEP AGSPRARYRK EQASTQPVPW IPPVDNLLKD
STDGSALGAL LHFYCPQLLP LDDVCLKENM SLADRLYNLQ LIQDFCKDNL NSCCHFSLED
MLYASSTVKN NYLAFMAELF WWFEVVKPSF VEPRKLDTEG TGKCEILTLQ LYLYSIFQRD
TNCFTHSVVI VTHHMRLTGE IKRSTSMSFV DGNLGTWPKE KRSGPYGVSF DIPFDKEESA
PATVPSTRGM VRSVSTDDGS GFKVLHMPRG MKRNLSFQPV NGQSVGIEEE GCPDSLAGME
PSKQGYSNGH RGVTETTPST EEALQIIQSP TRPPVEGINN GFFLHSQEHG AGVGALDPVS
EVDSKGPLST TDTTEVDTGI HIQTEDMLDE DSSLKDCSVN MELDMDTPSP CPSSQSKSPS
AVKMTSFAEQ KMKKLNPSAP DSGRGSCSSL KTTPEGSEFG LPLSVSWAPT PEHSPLPPND
PAQVMATEMV QLRMRLEEKR KAIEAQKKKV EAAFTRHRQK MGHSAFLNVV KRKGDGAASG
EEGGKTEGEG KSASTSPTFK FGRNKADTPD GAEQSSTASC WQKSPGAGEE GGQSHAQLTE
VDLTEYTRSI EKLNHSLAFL QTEMQRLAQQ QEVIMAMREQ KQQQAWVIPP PHTNPSPQKH
GRAGAVTRSS GPSSPADSPR STHRSPTSIK RKSASFHSRN PRTPRPSELK LAPYSRVLTA
PQSVDSIPRL RRFSPCQPLA KQSETTDMET DYQKAQKSDI ELKPTLESTF PEVLAHPVIE
TFTVMPTEIP FQSELSGQAK SSLIEVPLSV VKPLEDPTLD ESLEMQQGDA ESLDDEQKLC
RGFFFKEDGK AEENMAQKRA ALLEKRMRRE KESQQKKMQL EAELEQKKEE ARLKAEEERV
RKEEDKARKE FIKQEYLRRK QLKLMEDMDT VIKPRPAAGA KQRRGRPKSI HRDSMDSPKT
PVRAATVSSL SLASLNLGDN DSVHSEKRAA RPDSADGFLS PSRSSSRNGE KDWENGSTTS
SVTSNTEYTG PRLYKEPSAK SNKHIIQNAL AHCCLAGKVN EGQKNKILEE MEKSEANNFL
VLFRDAGCQF RALYTYCPET EEINKLTGIG PKSITRKMID GLYKYNSDKK QFSQIPAKTM
SASVDAVTIH NHLWQTKKPA TPKKVVPAQS
//
