GenomeNet

Database: UniProt
Entry: A0A2Y9TE92_PHYMC
LinkDB: A0A2Y9TE92_PHYMC
Original site: A0A2Y9TE92_PHYMC 
ID   A0A2Y9TE92_PHYMC        Unreviewed;      1472 AA.
AC   A0A2Y9TE92;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 2 isoform X3 {ECO:0000313|RefSeq:XP_023986424.1};
GN   Name=CAMSAP2 {ECO:0000313|RefSeq:XP_023986424.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023986424.1};
RN   [1] {ECO:0000313|RefSeq:XP_023986424.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023986424.1};
RG   RefSeq;
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   RefSeq; XP_023986424.1; XM_024130656.3.
DR   KEGG; pcad:102986253; -.
DR   Proteomes; UP000248484; Chromosome 4.
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:UP000248484}.
FT   DOMAIN          211..324
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1332..1466
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          361..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          784..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          744..771
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        579..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..818
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..862
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..927
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1059
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1174..1233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1472 AA;  162972 MW;  998EBB54C3A8809B CRC64;
     MGDAADPRDG RRTFIVPDIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELREPFYTD
     QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
     VTERDLHKKP IQMSAHLAMM DTLMMAYTVE MVSVEKVAAC AQQYSAFFQA TDLPYDIEDA
     VMYWINKVNE HLKDIMEQEQ KLKDHHTVEA SGGQKARYRK EQTLLKQLPC IPLVENLLKD
     GSDGCALAAL IHFYCPGVVR LEDICLKETM SLADSLYNLQ LIQEFCQEYL NQCCHFSLED
     MLYAASSIKS NYLVFMAELF WWFEVVKPSF VQPRDARPQG AEPVDDLPSV PVLTAAQRNA
     LDSSDFTPSG EGAVLTHSRP HLPSRHSRPP AHPSASGGIR RSSSMSYVDS FIGTWPKEKR
     SSVHGVSFDI SFDKESSIQR STPNRGITRS ISNEGLTLNN SRVSRNIRKN LSFKPVNGEE
     GAGSIEEELH VGPHGHLAAC VPRNTNELDC KQNMHHRLPN GALQNRALLD EFGSQVGTPS
     IEEALQIIHD TEKPAHTPRP DQLANGFFLH SQEMGVLSAG VPRSQSSPEG VADTKGASSP
     VTDNTEADTG IHVPSEDIPE TMDEDSSLRD YTVSLDSDVD DTSKFLQDYN AREALSPCPS
     TVSTKSQPGS STSSSSGVKM TSFAEQKFRK LNHTDGRSSG SSSQKTTPEG SELNIPHVVA
     WAQTAEDTGL PHGRDTTQLL ASEVVHLRMK LEEKRRAIEA QKKKMEAAFT KQRQKMGRTA
     FLTVVKRKGD GPSPPREEAA GAEDGKAYAE RPPEKEPQKA NGPRSGSPAD PKEGAESPVG
     RWPPSPSAPG DPEGPWSPAG PAEEPPQDGE LLEHTRSIER LNASLLVLQR EMQRLALQQE
     LLMHMREQQA WVISPPPPPP SPSPHRPARA GKPHRPPADG PRPAHASPQP QPAARKSAAP
     SVKAQRTPRP SELKLTPLHR TLTPPRSVDS LPRLRRFSPS QVPIQTRSFV CLGGGGEPEA
     KESRREEEGG GEEEGEGSAG PRGQRGHVPE DEDEEARALP SAAPEGLAQP ATETAWPSLG
     EDCVTHPAEP PSRPAFPAAP PKSANLIEVS LSDLKAPEKA DVSVEKYDGE SDKEQVDDDQ
     KVCCGFFFKD DQKAENDMAM KRAALLEKRL RREKETQLRK QQLEAEMEHK KEETRRKTEE
     ERQKKEDERA RREFIRQEYL RRKQLKLMED MDTVIKPRPQ GAKQKKQRPK SIHRDHIESP
     KTPIKGPPVS SLSLASLNTG DSESVHSGRR TPRSESVEGF LSPSRCGSRN GEKDWENAST
     TSSVASGTEY TGPKLFKEPS AKSNKHIIQN ALAHCCLAGK VNEGQKKKIL EEMEKSDANN
     FLILFRDSGC QFRSLYTYCP ETEEINKLTG IGPKSITKKM IEGLYKYNSD RKQFSHIPAK
     TLSASVDAIT IHSHLWQTKR PVTPKKLLPT KA
//
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