ID A0A3B3TF61_9TELE Unreviewed; 1443 AA.
AC A0A3B3TF61;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 2-like {ECO:0000313|Ensembl:ENSPKIP00000041305.1};
GN Name=CAMSAP2 {ECO:0000313|Ensembl:ENSPKIP00000041305.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000041305.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000041305.1}
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 Ensembl; ENSPKIT00000022340.1; ENSPKIP00000041305.1; ENSPKIG00000017872.1.
DR GeneTree; ENSGT00950000182975; -.
DR Proteomes; UP000261540; 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: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..326
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1303..1437
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 461..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 714..745
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 825..862
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 487..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 160998 MW; 99D2D1543F937528 CRC64;
MGDVGSAKEI KKTFIVPAIK AFEHYDFTRA KICCSLTWLM AKAFGTDSVP TDLREPFYRD
QYEQEHIKPP VVSLLLSAEP YCRAGSLILK SDAAKPLLGH DAVIRALAQK GLYVTDQERL
VTERDLQKRP IQMSSHLAMI DTLMMAYTVE MVSVEKLLSC VQKYSPCYPD GDVPYDTEEA
VATWINKVNE NLRDIITQEQ KLRELSCADK DQAEDSPARY RKEQTISRQA PCLPLVDNLL
KDTADGCAIA ALLHFYCPDL VKLEDICLKE TMSLADSLFN LQLIQDFCGD NLDRCCHFTL
EDMVYASSSI KNNYLVFMAE LFWWFEVVKP SFVRPQMLRT EALEPSSLRG IPSVPISNAS
NRSFMENPPL PEHPSLPLRV QPQTSTSGII KRSTSLSYMD GCVGTWPKEK RSSAHGISFD
IPFDKEDTVK SSTISNRGMT RSISTDGLGF KVNHVSKNMK RNLSFQPVNG QSEREGIEEE
EPPVNLVGTN TERQPERSLP KNNKGLLNGQ VSDDHGNLPM PSMEEALKII HDSERPQGSI
QGEAVDNGFF LHGLETGDLC PKARGAEADT DSVSTEVDTG IHVRTEDIQE TLDEDSSLKD
YTVSLDSDMD HDFELRVSKA REMTSPCPSS MSARSHADST ASSSSGVKMT SFAEQKFKKL
NHVEGRSTSS SSPKTTPESS ELNIPHMVGW APMAQESPIR QSPRDPTQML ASEMVHLKMK
LEEKRRAIEA QKKKVEEAFT RHRQKMGRTA FLNVVRKKGG ATSPLKDEAG AGEGNSSFGD
HQSNKPPANG SQQPVKGKLE GEDTDRSQVT WMKSSSDESA SEVDMAEYTK SIEKLNASLN
FLQVEMQRLA QQQEVIMQMR DQQSWVISPP QPSPQKQVQD LRHSTRSAGS MSPVLSSAGS
PRPAHRSPAA IKRKSASFHS RTPRTPRPSE LRITPFNRML NTPQSVDSLP RLRKFSPSQT
QTTSYTYLGH DSRPTRGPDP KPEESTQSTK NGQPAAETPA QATIAVDPAP APTKETKQKE
QDRRAVVDLR EGSKPRESKV SEVLTQPVTE TFTVIPSANP TGATGPTAKN LIEVPLSVLK
PLEGQGLEKD ESGAGEEVSK EEQKTCCGFF FKDDMKGEED IALKRAALLE KRLRRERETQ
QKKQQQEAEQ EQRKEMTRMK AEEERQKKED EKARKEFIKQ EYLRRKQLKL MEDMDSVIKP
RPLSAKQKKP RPKSIHRDVM ESSKPSAKAT AGSRPRVHSV SSLSLASLNL RDSESLQSER
VLPRPDSADG CLSPCRSGSR NGEKDWENGS TTSSVASNTE YTGPKLYKEP SAKSNKHIIQ
NALAHCCLAG KVNEGQKNKI LEEMEKSEAN NFLILFRDSG CQFRSVYTYF PETEEITKLA
GIGPKTITHK MIEGLYKYNS DRKQFSHIPA KTMSASVDAV TIYSHLWQTK KPGTPKKVLS
TKS
//
