ID A0A6P6J8K4_CARAU Unreviewed; 1433 AA.
AC A0A6P6J8K4;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE SubName: Full=Calmodulin-regulated spectrin-associated protein 3-like isoform X1 {ECO:0000313|RefSeq:XP_026056708.1, ECO:0000313|RefSeq:XP_026056716.1};
GN Name=LOC113042248 {ECO:0000313|RefSeq:XP_026056708.1,
GN ECO:0000313|RefSeq:XP_026056716.1, ECO:0000313|RefSeq:XP_026056725.1};
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957 {ECO:0000313|Proteomes:UP000515129, ECO:0000313|RefSeq:XP_026056725.1};
RN [1] {ECO:0000313|RefSeq:XP_026056708.1, ECO:0000313|RefSeq:XP_026056716.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026056708.1,
RC ECO:0000313|RefSeq:XP_026056716.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026056708.1,
RC ECO:0000313|RefSeq:XP_026056716.1};
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_026056708.1; XM_026200923.1.
DR RefSeq; XP_026056716.1; XM_026200931.1.
DR RefSeq; XP_026056725.1; XM_026200940.1.
DR Ensembl; ENSCART00000127363; ENSCARP00000113823; ENSCARG00000058655.
DR GeneID; 113042248; -.
DR KEGG; caua:113042248; -.
DR OrthoDB; 2125658at2759; -.
DR Proteomes; UP000515129; Chromosome 3.
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:UP000515129}.
FT DOMAIN 218..328
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1294..1428
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 188..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..888
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..978
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1270
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 158103 MW; 23E42F510F3C28FE CRC64;
MVDSNAMRKT FVVPDIKPLD QYDLTRARIC ASVGWLLGKS YGNAENVPVE LRDPFYCDQY
EQEHLKPPVT RLLLSPELYC RTYGLLLGGS PGAEGPPKDI PALLQVLGRK GLAPKDQNAP
VTEAELRQKP IKMSAHLELI DALMAVGAME MVSRVLASGG SELLGTDASW DRALLYWVNT
LNQKLKEQTE GTLNDASQPS TEPQPVQPSC PTRWYWKLVP ILYRKDRMQS KLKPYFPVVN
EVKDLSNGCA IAAVIHYYCP GLLRLEDVCM KDSMSVADSL YNLQLIREFC DSCLKSCCPL
ALEDLLYSPA ELKTNILSFL AELLYWFEVS KPEFVQPLQD SELTETSGRT GNGNSGSSNS
GSPSIFKRPF LPISSPVTAA TGSLTQSTSM SHVETAGRTW TKKPLSRPLS AVSFSIPFGL
DSDVDIVMGN PVITRSVSSD NLNPAGQSMT REPYTPPEDL SHLLSKAPGP NGPQRASWAT
QTRPLLAEEN GIDDSETGEL PTIEEALQII HNEEKMEPRL HPDGAPDGFY LHSLDDPANA
RLNGSPVTLS SSAPSRSGML YNRSSGIPPE PSRTRHPSEG SRDDDSVLRD GSMDSDASED
LPKIHSTPAT PASGPRITEP RCVKTPESGV RMTNFAERKK KLVPEQVQPS EPQVPQMTTW
AKKLEESPSK SPAVSTEMSE LGARLEEKRK AIEAQKKRIE AIFAKHRQRL GKSAFLQLKK
EQEDGDGEEG RQGEVGTSSI ENDLSRLALE EKLARLESEE EQDEQQQEQL KKGPSVEEEG
NIKSHVQQDN PVEKEKAGVG IPGGKETAPL GNYNNAVSKL SAALNSLQND MQRLSEQQNQ
LMKKKVAPNI QASGVPPSPK PSTAASSRLS RESNRNLSSA SSSPSPSRKI ANHTAPPKSP
SSHRRAQSAP PKSPKLHHPR PAELKTPAST RVITLPQNVD NIPHLRRVSP WQCRDQNSSS
FSIGTSSQSE SRSASSLART EDNISDTGSS EDHTIFSMEL DSGSSQVLAR KDRQGGGSSS
GAPSECSFES DLPAAGFNGK HKSLIEISLS SLKALEGEGA DQSQDNFSDS MSDQTEPEIS
GGVGFFFKQD EARPEDEMER RRAALLEKQQ KRAEEIKRRR QEQEREREPS RSSSMDESRR
GEERPQTPST PPPPRTPPPE GTPQRRGDFT RQEYERRHQL KIMEDLDKVL RQKPTTVRGV
KKQRPKTVFR DDSDLSRSPA KGFMGSRLNK VYSHSTTNLS SMANDNGTLT VRKSPSRSHS
PSRLLSPGRL AAQNGDWENE STISSAASIP EYTGPKLYKE PSFKSNKFII HNAISRCCLA
GKVNEPQKNK IVEEMEKSPA NHFLILFRDA SCQFRAVYTM NPETEEMVRL VGVGPRVINL
TMVESIYKYS SDRKQFTTIP SKTMSMSVDA FTIPGHLWER KRPGTPKKLG TPK
//
