ID A0A2I3RE09_PANTR Unreviewed; 1489 AA.
AC A0A2I3RE09; A0A2J8KHV0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Calmodulin regulated spectrin associated protein family member 2 {ECO:0000313|Ensembl:ENSPTRP00000062878.1};
GN Name=CAMSAP2 {ECO:0000313|Ensembl:ENSPTRP00000062878.1,
GN ECO:0000313|VGNC:VGNC:5000};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000062878.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000062878.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000062878.1}
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; AACZ04071406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001144062.1; XM_001144062.3.
DR STRING; 9598.ENSPTRP00000062878; -.
DR Ensembl; ENSPTRT00000110987.1; ENSPTRP00000062878.1; ENSPTRG00000001822.7.
DR GeneID; 457611; -.
DR CTD; 23271; -.
DR VGNC; VGNC:5000; CAMSAP2.
DR GeneTree; ENSGT00950000182975; -.
DR InParanoid; A0A2I3RE09; -.
DR OrthoDB; 2918432at2759; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001822; Expressed in temporal lobe and 21 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0036449; C:microtubule minus-end; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IBA:GO_Central.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0061564; P:axon development; IEA:Ensembl.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR GO; GO:1903358; P:regulation of Golgi organization; IEA:Ensembl.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IEA:Ensembl.
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:UP000002277}.
FT DOMAIN 222..335
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1349..1483
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 375..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 761..788
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 888..925
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 670..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1489 AA; 168143 MW; 1724E3EAB2D7B015 CRC64;
MGDAADPREM RKTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELQEPFYTD
QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MVSIEKVIAC AQQYSAFFQA TDLPYDIEDA
VMYWINKVNE HLKDIMEQEQ KLKEHHTVEA PGGQKSPSKW FWKLVPARYR KEQTLLKQLP
CIPLVENLLK DGTDGCALAA LIHFYCPDVV RLEDICLKET MSLADSLYNL QLIQEFCQEY
LNQCCHFTLE DMLYAASSIK SNYLVFMAEL FWWFEVVKPS FVQPRVVRPQ GAEPVKDMPS
IPVLNAAKRN VLDSSSDFPS SGEGATFTQS HHHLPSRYSR PQAHSSASGG IRRSSSMSYV
DGFIGTWPKE KRSSVHGVSF DISFDKEDSV QRSTPNRGIT RSISNEGLTL NNSRVSKHIR
KNLSFKPING EEEAESIEEE LNIDSHSDLK SYVPLNTNEL NSNENIHYKL PNGALQNRIL
LDEFGNQIET PSIEEALQII HDTEKSPHTP QPDQIANGFF LHSQEMSILD SNIKLNQSSP
DNVTDTKGAL SPITDNTEVD TGIHVPSEDI PETMDEDSSL RDYTVSLDSD MDDASKFLQD
YDIRTGNTRE ALSPCPSTVS TKSQPGSSAS SSSGVKMTSF AEQKFRKLNH TDGKSSGSSS
QKTTPEGSEL NIPHVVAWAQ IPEETGLPQG RDTTQLLASE MVHLRMKLEE KRRAIEAQKK
KMEAAFTKQR QKMGRTAFLT VVKKKGDGIS PLREEAAGAE DEKVYTDRAK EKESQKTDGQ
RSKSLADIKE SMENPQAKWL KSPTTPIGPE KQWNLASPSE ETLNEGEILE YTKSIEKLNS
SLHFLQQEMQ RLSLQQEMLM QMREQQSWVI SPPQPSPQKQ IRDFKPSKQA GLSSAITPFS
SDSPRPTHPS PQSSNRKSAS FSVKSQRTPR PNELKITPLN RTLTPPRSVD SLPRLRRFSP
SQVPIQTRSF VCFGDDGEPQ LKESKPKEEV KKEELESKGT LEQRGHNPEE KEIKPFESTV
SEVLSLPITE TVCLTPNEDQ LNQPTEPPPK PVFPPTAPKN VNLIEVSLSD LKPPEKADVP
VEKYDGESDK EQFDDDQKVC CGFFFKDDQK AENDMAMKRA ALLEKRLRRE KETQLRKQQL
EAEMEHKKEE TRRKTEEERQ KKEDERARRE FIRQEYMRRK QLKLMEDMDT VIKARPQVVK
QKKQRPKSIH RDHIESPKTP IKGPPVSSLS LASLNTGDNE SVHSGKRTPR SESVEAFLSP
SRCGSRNGEK DWENASTTSS VASGTEYTGP KLYKEPSAKS NKHIIQNALA HCCLAGKVNE
GQKKKILEEM EKSDANNFLI LFRDSGCQFR SLYTYCPETE EINKLTGIGP KSITKKMIEG
LYKYNSDRKQ FSHIPAKTLS ASVDAITIHS HLWQTKRPVT PKKLLPTKA
//
