ID A0A455B7U1_PHYMC Unreviewed; 1480 AA.
AC A0A455B7U1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 2 isoform X2 {ECO:0000313|RefSeq:XP_028344063.1};
GN Name=CAMSAP2 {ECO:0000313|RefSeq:XP_028344063.1};
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_028344063.1};
RN [1] {ECO:0000313|RefSeq:XP_028344063.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028344063.1};
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_028344063.1; XM_028488262.2.
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 222..335
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1340..1474
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 372..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 755..782
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 590..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 164078 MW; 4666CBAF2A88A117 CRC64;
MGDAADPRDG RRTFIVPDIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELREPFYTD
QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
VTERDLHKKP IQMSAHLAMM DTLMMAYTVE MVSVEKVAAC AQQYSAFFQA TDLPYDIEDA
VMYWINKVNE HLKDIMEQEQ KLKDHHTVEA SGGQKSPSKW FWKLVPARYR KEQTLLKQLP
CIPLVENLLK DGSDGCALAA LIHFYCPGVV RLEDICLKET MSLADSLYNL QLIQEFCQEY
LNQCCHFSLE DMLYAASSIK SNYLVFMAEL FWWFEVVKPS FVQPRDARPQ GAEPVDDLPS
VPVLTAAQRN ALDSSDFTPS GEGAVLTHSR PHLPSRHSRP PAHPSASGGI RRSSSMSYVD
SFIGTWPKEK RSSVHGVSFD ISFDKESSIQ RSTPNRGITR SISNEGLTLN NSRVSRNIRK
NLSFKPVNGE EGAGSIEEEL HVGPHGHLAA CVPRNTNELD CKQNMHHRLP NGALQNRALL
DEFGSQVGTP SIEEALQIIH DTEKPAHTPR PDQLANGFFL HSQEMGVLSA GVPRSQSSPE
GVADTKGASS PVTDNTEADT GIHVPSEDIP ETMDEDSSLR DYTVSLDSDV DDTSKFLQDY
NAREALSPCP STVSTKSQPG SSTSSSSGVK MTSFAEQKFR KLNHTDGRSS GSSSQKTTPE
GSELNIPHVV AWAQTAEDTG LPHGRDTTQL LASEVVHLRM KLEEKRRAIE AQKKKMEAAF
TKQRQKMGRT AFLTVVKRKG DGPSPPREEA AGAEDGKAYA ERPPEKEPQK ANGPRSGSPA
DPKEGAESPV GRWPPSPSAP GDPEGPWSPA GPAEEPPQDG ELLEHTRSIE RLNASLLVLQ
REMQRLALQQ ELLMHMREQQ AWVISPPPPP PSPSPHRPAR AGKPHRPPAD GPRPAHASPQ
PQPAARKSAA PSVKAQRTPR PSELKLTPLH RTLTPPRSVD SLPRLRRFSP SQVPIQTRSF
VCLGGGGEPE AKESRREEEG GGEEEGEGSA GPRGQRGHVP EDEDEEARAL PSAAPEGLAQ
PATETAWPSL GEDCVTHPAE PPSRPAFPAA PPKSANLIEV SLSDLKAPEK ADVSVEKYDG
ESDKEQVDDD QKVCCGFFFK DDQKAENDMA MKRAALLEKR LRREKETQLR KQQLEAEMEH
KKEETRRKTE EERQKKEDER ARREFIRQEY LRRKQLKLME DMDTVIKPRP QGAKQKKQRP
KSIHRDHIES PKTPIKVSSL SLASLNTGDS ESVHSGRRTP RSESVEGFLS PSRCGSRNGE
KDWENASTTS SVASGTEYTG PKLFKEPSAK SNKHIIQNAL AHCCLAGKVN EGQKKKILEE
MEKSDANNFL ILFRDSGCQF RSLYTYCPET EEINKLTGIG PKSITKKMIE GLYKYNSDRK
QFSHIPAKTL SASVDAITIH SHLWQTKRPV TPKKLLPTKA
//
