ID I3MKB0_ICTTR Unreviewed; 1464 AA.
AC I3MKB0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Calmodulin regulated spectrin associated protein family member 2 {ECO:0000313|Ensembl:ENSSTOP00000011705.3};
GN Name=CAMSAP2 {ECO:0000313|Ensembl:ENSSTOP00000011705.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011705.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011705.3}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AGTP01062308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005330433.1; XM_005330376.2.
DR Ensembl; ENSSTOT00000013061.3; ENSSTOP00000011705.3; ENSSTOG00000013058.3.
DR GeneID; 101954658; -.
DR CTD; 23271; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR OrthoDB; 2918432at2759; -.
DR TreeFam; TF315529; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 211..324
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1324..1458
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 574..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 736..763
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 863..900
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 574..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1464 AA; 165517 MW; 2587C7C9B5DC301D CRC64;
MGDAADPREM RKTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELREPFYTD
QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MVSIEKVIAC AQQYSAFFQA TDLPYDIEDA
VMYWINKVNE HLKDIMEQEQ KLKEHHTVET PGGQKARYRK EQTLLKQLPC IPLVENLLKD
GTDGCALAAL IHFYCPGVVR LEDICLKETM SLADSLYNLQ LIQEFCQEYL NQCCHFTLED
MLYAASSIKS NYLVFMAELF WWFEVVKPSF VQPRVVCPQG AEPVKDMPSI PVLNAAKRNV
LDSSCSSDFT SRYSRPQAHS SASGGIRRSS SMSYVDGFIG TWPKEKRSSV HGVSFDISFD
KEDSEQRSTS NRGITRSISN EGLTLNNNRV SKHIRKNLSF KPVNGEEEAE SIEEELNIDS
QSDFKSYVPL NTNELNSNEN IHYKLPNGAL QNRVLLDEFG NQIETPSIEE ALQIIHDTER
SPHTPRPDQI ANGFFLHNQE MSILNSNIKL NQSSPDNITD TKGALSPITD TTEVDTGIHV
PSEDIPETMD EDSSLRDYTV SLDSDMDDAS KFLQDYDIRT SNPRDALSPC PSTISTKSQP
GSSASSSSGV KMTSFAEQKF RKLNHTDGKS SGSSSQKTTP EGSELNIPHV VAWAQIPEET
GLPQARDTTQ LLASEMVHLR MKLEEKRRAI EAQKKKMEAA FTKQRQKMGR TAFLNVVKKK
GDGISPLREE AAGAEDEKVY TDRTKEKESQ KTDGQRSKSL ADIKESMENP PAKWLKSPTT
PVDPEKQWNL ASPSEETLNE GEILEYTKSI EKLNSSLHFL QQEMQRLSLQ QEMLMQMREQ
QSWVISPPQP SPQKQIRDFK PSRQAGLSSA IAPFSSDSPR PTHPSPQSSN RKSTSFSVKN
QRTPRPNELK ITPLNRTLTP PRSVDSLPRL RRFSPSQVPI QTRSFVCFGD DGEPQLKESK
PKEEVKKDEL ECKGTLEQHG HNLEEKELKP FESTVSEVLS QPITETVCLT PNEDQLSQPT
EPPPKPVFPP TAPKNVNLIE VSLSDLKPPE KADESVEKYD GESDKEPLED DQKVCCGFFF
KDDQKAENDM AMKRAALLEK RLRREKETQL RKQQLEAEME HKKEETRRKT EEERQKKEDE
RARREFIRQE YMRRKQLKLM EDMDTVIKPR PQMAKQKKQR PKSIHRDHIE SPKTPIKGPP
VSSLSLASLN TGDNESVHSG KRTPRSESVE AFLSPSRCGS RNGEKDWENA STTSSVASGT
EYTGPKLYKE PSAKSNKHII QNALAHCCLA GKVNEGQKKK ILEEMEKSDA NNFLILFRDS
GCQFRSLYTY CPETEEINKL TGIGPKSITK KMIEGLYKYN SDRKQFSHIP AKTLSASVDA
ITIHSHLWQT KRPVTPKKLL PTKA
//
