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Database: UniProt
Entry: A0A2U3VDQ7_ODORO
LinkDB: A0A2U3VDQ7_ODORO
Original site: A0A2U3VDQ7_ODORO 
ID   A0A2U3VDQ7_ODORO        Unreviewed;      1490 AA.
AC   A0A2U3VDQ7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 2 isoform X1 {ECO:0000313|RefSeq:XP_004392785.1};
GN   Name=CAMSAP2 {ECO:0000313|RefSeq:XP_004392785.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004392785.1};
RN   [1] {ECO:0000313|RefSeq:XP_004392785.1}
RP   IDENTIFICATION.
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_004392785.1; XM_004392728.2.
DR   STRING; 9708.A0A2U3VDQ7; -.
DR   GeneID; 101384099; -.
DR   KEGG; oro:101384099; -.
DR   CTD; 23271; -.
DR   InParanoid; A0A2U3VDQ7; -.
DR   OrthoDB; 2918432at2759; -.
DR   Proteomes; UP000245340; Unplaced.
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:UP000245340}.
FT   DOMAIN          222..335
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1350..1484
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          387..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1192..1350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          762..789
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          889..926
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        401..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..1008
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1078
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1192..1251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1287..1303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1490 AA;  168004 MW;  A760CEFF96BE8D68 CRC64;
     MGDAADPREM KKTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELREPFYTD
     QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
     VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MVSIEKVIAC AQQYSAFFQA TDLPYDIEDA
     VMYWINKVNE HLKDIMEQEQ KLKEHHTVEA PGGQKSPSKW FWKLVPARYR KEQTLLKQLP
     CIPLVENLLK DGTDGCALAA LIHFYCPGVV RLEDICLKET MSLADSLYNL QLIQEFCQEY
     LNQCCHFTLE DMLYAASSIK SNYLVFMAEL FWWFEVVKPS FVQPRVVRPQ GAEPVNDMPS
     IPVLNAAKTN ILDSSCSSDF TSSGEGAAFT HSHHLPSRHS RSQAHSSASG GIRRSSSMSY
     VDGFIGTWPK EKRSSVHGVS FDISFDKENT VHRSTPNRGI TRSISNEGLT LNNNRVSKNI
     RKNLSFKPVN GEEEAESIEE ELNIDSHSGL KSYTLLNTNE LNSNENIHYK LPNGALQNRV
     LLDEFGNQIE TPSIEEALQI IHDTEKSPHT SQPDHIANGF FLHNQEMSIL NSNIKLNQSS
     PDNITDTKGA LSPITDNTEV DTGIHVPSED IPETMDEDSS LRDYTVSLDS DMDDASKFLQ
     DYDIRTSNPR EALSPCPSTV STKSQPGSSA SSSSGVKMTS FAEQKFRKLN HTDGKSSGSS
     SQKTTPEGSE LNIPHVVAWG QIPEEAGLPQ GRDTTQLLAS EMVHLRMKLE EKRRAIEAQK
     KKMEAAFTKQ RQKMGRTAFL TVVKKRGDGI SPLREEAAGA EDEKVYTDRA KEKDSQKANG
     QRSKSLADLK ESMENPQAKW LKSPTTPIDP EKQWNLASPS EETLNEGEIL EYTKSIEKLN
     SSLHFLQQEM QRLSLQQEML MQMREQQSWV ISPPQPSPQK QIRDFKPSRQ AGLSSASAPF
     SSDAPRPTHP SPQSSNRKNT SFSVKNQRTP RPNELKITPL NRTLTPPRSV DSLPRLRRFS
     PSQVPIQTRS FVCFGDDGEP QLKESKPKEE VKKEELESKG PVGQHVRNPE EKEIRPLEST
     VSEVLSQPIT ETVRLTPNED QLNQPAEPPP KPVFPPAAPK NVNLIEVSLS DLKPPEKADV
     SVEKYDGESD KEQFDDDQKV CCGFFFKDDQ KAENDMAMKR AALLEKRLRR EKETQLRKQQ
     LEAEMEHKKE ETRRKTEEER QKKEDEKARR EFIRQEYMRR KQLKLMEDMD TVIKPRPQIA
     KQKKQRPKSI HRDHIESPKT PIKGPPVSSL SLASLNTGDN ESVHSGKRTP RSESVEGFLS
     PSRCGSRNGE KDWENASTTS SVASGTEYTG PKLYKEPSAK SNKHIIQNAL AHCCLAGKVN
     EGQKKKILEE MEKSDANNFL ILFRDSGCQF RSLYTYCPET EEINKLTGIG PKSITKKMIE
     GLYKYNSDRK QFSHIPAKTL SASVDAITIH SHLWQTKRPV TPKKLLPTKA
//
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