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Database: UniProt
Entry: A0A3Q0DHD9_MESAU
LinkDB: A0A3Q0DHD9_MESAU
Original site: A0A3Q0DHD9_MESAU 
ID   A0A3Q0DHD9_MESAU        Unreviewed;      1263 AA.
AC   A0A3Q0DHD9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 27.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 3 isoform X4 {ECO:0000313|RefSeq:XP_021091739.1};
GN   Name=Camsap3 {ECO:0000313|RefSeq:XP_021091739.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021091739.1};
RN   [1] {ECO:0000313|RefSeq:XP_021091739.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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_021091739.1; XM_021236080.1.
DR   AlphaFoldDB; A0A3Q0DHD9; -.
DR   Ensembl; ENSMAUT00000013088; ENSMAUP00000009242; ENSMAUG00000010380.
DR   GeneID; 101831803; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0036449; C:microtubule minus-end; IEA:TreeGrafter.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0051011; F:microtubule minus-end binding; IEA:TreeGrafter.
DR   GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:TreeGrafter.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:TreeGrafter.
DR   GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR   FunFam; 3.10.20.360:FF:000001; Calmodulin-regulated spectrin-associated protein 3 isoform 2; 1.
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:SF2; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 3; 1.
DR   PANTHER; PTHR21595; PATRONIN; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW   ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT   DOMAIN          219..328
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1123..1257
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          183..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..367
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..389
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..756
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..785
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..951
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..982
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1263 AA;  136287 MW;  E7E422A706D6047C CRC64;
     MVEAAPAGSG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE HVPPELWEPF
     YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLEPPPN PSALLALLAR RGTVPSLPEH
     PVREADLRHQ PILMGAHLAV IDALMVAFSF EWTKTLPGPL ALSSLEHKLL FWVDTTVRRL
     QEKTEQEAAQ RASPAAPLDG AAPAQPSHAI AFCLKESGNK PPMIRYRKDR AIARRAPCFP
     NVTTLQDLAS GAALAATIHC YCPQLLRLEE VCLKDPMSVA DSLYNLQLVQ DFCASHLPRG
     CPLSLEDLLY VPPPLKVNLV VLLAEMYMCF EVLKPDFVQA KDLPDGHASS PRGTETLSSQ
     NNSGSSSPVF NFRHPLLSPG GPQSPLRGST GSLKSSPSMS HMEALGKAWN RQLSRPLSQA
     VSFSTPFGLD SDVDVVMGDP VLLRSVSSDS LGPPRPVSSS SRNPVQATPE SGDLPTIEEA
     LQIIHSAEPR LLPDGAADGS FYLHSPEGLS KPPLASPYPP EGASKPPSDG LNKAPIYISH
     PETPVKPSPC PAGEVLKPLP PSEGSPKAVA SSPAANNSEV KMTSFAERKK QLVKAEAESG
     MGSPTSTPAA PEALSSEMSE LGARLEEKRR AIEAQKRRIE AIFAKHRQRL GKSAFLQVQP
     REAAGEAEEE AELGSVPGGE RPAGEGQGEP SSRPKSVTFS PDLGPVPPEG LGDYNRAVSK
     LSAALSSLQR DMQRLTDQQQ RLLAPPEAPG PAPPPAAWVI PGPTTGPKAA SPSPARRAPA
     ARRSPGPGPN PTPRSPKHTR PAELKLAPLT RVLTPPHDVD SLPHLRKFSP SQVPVQTRSS
     ILLSEGTPPE EPTTKPALIE IPLASLGEPT ADEEGDGSPA GAEDSLEEEA SSEGEPRSGL
     GFFYKDEDKP EDEMAQKRAS LLERQQRRAE EARRRKQWQE AEKEQKREEA AARLAQEEVP
     ATPVASTAPV ATLAPATRAA APAEEEVGPR RGDFTRLEYE RRAQLKLMDD LDKVLRPRAC
     GPGRGGRRAT RPRSGCCDDS ALARSPARGL LGSRLSKVYS QSTLSLSTVA NEASNNLGVK
     RPTSRAPSPS GLMSPSRLPG SRERDWENGS NASSPASVPE YTGPRLYKEP SAKSNKFIIH
     NALSHCCLAG KVNEPQKNRI LEEIEKSKAN HFLILFRDSS CQFRALYTLS GETEELSRLA
     GYGPRTVTPA MVEGIYKYNS DRKRFTQIPA KTMSMSVDAF TIQGHLWQSK KPTTPKKGGG
     TPK
//
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