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Database: UniProt
Entry: A0A1S3R7U7_SALSA
LinkDB: A0A1S3R7U7_SALSA
Original site: A0A1S3R7U7_SALSA 
ID   A0A1S3R7U7_SALSA        Unreviewed;      1519 AA.
AC   A0A1S3R7U7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Calmodulin-regulated spectrin-associated protein 3-like isoform X3 {ECO:0000313|RefSeq:XP_014048196.1};
GN   Name=LOC106600930 {ECO:0000313|RefSeq:XP_014048196.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014048196.1};
RN   [1] {ECO:0000313|RefSeq:XP_014048196.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014048196.1};
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_014048196.1; XM_014192721.1.
DR   STRING; 8030.ENSSSAP00000028490; -.
DR   PaxDb; 8030-ENSSSAP00000028490; -.
DR   GeneID; 106600930; -.
DR   CTD; 57662; -.
DR   OrthoDB; 2918432at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa03.
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:SF2; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 3; 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:UP000087266}.
FT   DOMAIN          248..362
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1380..1514
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          223..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          779..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1221..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1323..1377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1175..1210
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        227..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..987
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1047
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1323..1353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1519 AA;  165758 MW;  3558500A984D43A7 CRC64;
     MLDLNLFLSP PTIFKVSIPL RLPRPVCGLA MVDSNAMRKT FVVPDIKPLD LYDCTRAKIC
     ASVGWVLAKS YGNAEHVPVE LREPFYCDQY EQEHLKPPVT RLLLSSELYC RTYGLLQGDQ
     GGSGAPKDNA TLLQLLANRG VTPKDQDVPV TDEDLRHKPI KMSAHLAVMD ALMSVGAMET
     VSAVRMSGAA TGEELLGGVG EASWENTLLH WVNGLNQRLR EQTEGALGDP SQDSTEPQPV
     QPSCPTRWYW KLVPIRYRKD KTLSKQKPTF PVVTEVKDLS NGCAIAAIVH YYCPGLLQLE
     DVCMKESMAV EDSLYNLQLI REFCDSCLKS CCPLVLEDLL YTPQELQVNT MSFLAELLGW
     FEVRRPEFVQ PLNTTDASAT LKPTSLSNNS GSPSIFKKPF LPISSPVSPG PAPERAGRTW
     TKKPFSRPLS SAVSFSIPFG LDSDVDVVMG GAITRSVSSD NVAPGLTITR VPYTPPEDLS
     HLLSKPPAPP GSHRGSWATQ SSSVVPMLLK ENGLGDGEGD GELPTIEEAL QIIHNEDKME
     PRLHPDGAAD GFFLHSPDDP ASARRNGRAA HPSHPPNPIP LSCSAPSHSG MMYYPHTPMG
     GKTQQPREQP SSTPSSRTRH TSEGSRDDDS VLRDGSVDSD ASEDLLLLPN AQSTPATSAV
     HARSCGGGGD APDSGVRMTS FAERKKKPST VGESPKSGGA SSSEPVAPAA TAPMTSWVAQ
     PQKSTEESPS KSPGLTTEMS ELGARLDEKR KAIEAQKKRI EAIFAKHRQR LGKSAFLQLK
     KDQGVGERAE EEGGQVSASS TEEDLRGLTL DERLARMEDE EQQEERRLSL EQEGNVKPSS
     HLDNKQASLP RREKGAGAAG PAGPGGEQAG VVARQPAPLG DYNNAVSKLN AALSSLQSDM
     QRLSEQQNQL IRKKPVAPAG NKSWVIPPSL KSQAPPPTRM SRASTPRDLA SASSSPSSSR
     RNAASPGRTS KSPQVQRRAQ SVPPKSPKHQ ATHYHHARPQ DLKVPGLSRV LTPPQNVDTI
     PHLRRASPWQ CRDQNSSTFN ISSAPSPAST PTPTPTPRAL SLALDDNMSD AGSNEDQSIF
     SIDLDTATSQ ASGRKEHGGG GSSGAPSECS FESDVPAAGV FNGKRSSLIE ISLSALCGDE
     DDLSVMDDSM SDVTEPEMKG GVGFFFKDDK VRPEDEMAQR KAALMEKQRK RAEEMKRRRL
     EQEEKREKEH AIRPEWFNIE GWGDKCGGSG EDRTPGTPPS ESTSQRRDTF TRQEYERRQQ
     LKIMEDLDKV LRQKPTTVRG VKKQRPKTMF RDDSVLSRSP AKGFMGSKLN KVYSHSTMNL
     SSMANDTGNS GTLTVRKSPS RSHSPSRLMS PGRMANQNGE KDWENASTAS SPASIPEYTG
     PKLYKEPSFK SNKFIIHNAI SRCCLAGKVN EPQKNKIVEE MEKCQANHFL ILFRDSSCQF
     RAVYTMNPET EEMVRLTGIG PRVISPAMVE SIYKYSSDRK QFTTIPSKTM SMSVDAFTIP
     GHLWQSKRPG TPKKLGTPK
//
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