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
//