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Database: UniProt
Entry: A0A3P8ZFG1_ESOLU
LinkDB: A0A3P8ZFG1_ESOLU
Original site: A0A3P8ZFG1_ESOLU 
ID   A0A3P8ZFG1_ESOLU        Unreviewed;      1517 AA.
AC   A0A3P8ZFG1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSELUP00000027022.1};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000027022.1, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000027022.1, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000027022.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   Ensembl; ENSELUT00000017010.2; ENSELUP00000027022.1; ENSELUG00000003150.2.
DR   GeneTree; ENSGT00950000182975; -.
DR   Proteomes; UP000265140; LG13.
DR   Bgee; ENSELUG00000003150; Expressed in camera-type eye and 15 other cell types or tissues.
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   CDD; cd22265; UDM1_RNF168; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 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:SF3; CALMODULIN-REGULATED SPECTRIN-ASSOCIATED PROTEIN 1; 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:UP000265140}.
FT   DOMAIN          148..263
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          340..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          976..1172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          787..817
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        353..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..871
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1146..1161
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1283
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1517 AA;  166656 MW;  C535239B4FE97B10 CRC64;
     MFLTGNVSPL FVRMDLDLCA GGDSTRRKLD TAGEGAVEVV PLEMYDSARA KIDANLRWLF
     AKAYGIDHIP EDLRDPFYTD QYEQEHIKPP VLHLLLSCEL YCRVCALILK TDQAASLQSH
     MSVIQALSRK GIYVMESDDV PVTDADLACV PIKMVRYRRE HNTGRQLPFF PVLEDLMRDV
     CDGAALLTVV HYYCPDLMKL DDICLKEVTS IADSLYNIQL LKEFANEYLN KSFYLTMEDM
     LYSPLVLKHN VMVFIAELFW WFETVKPEFV QPRTDEFKDA RAMAQPKSAR PSVPISNATK
     RSFQVTPGMA EASLSVSAQS SPDVCNRYFL HPAEDCDPLK GGPAASFSPS HPLLPLRQRQ
     QKQQGEDGSG IRNRSNSLEN RQPRASVQAW PDKRQRPMST LNPYTFGISA TDSDADIASG
     DSVSLARSIS KDSLASNVAN LTPKHQSLTP QGHTLIGPAQ GVRPQVASAP QRVNGHGLLG
     NVDLEEEEEL EAVMRTEASP ALNNPLEARP AGAMPKDSFY LEPLMPAVLK PAKEKSVCLN
     KEEESGEAGR SRGAGSLRRA EGGPALATSA RRKTPNSLNR TYTPTSSGEL DMSTEAWLAG
     PPQGQGSFKP LVTSSAEPPG GFYLHSDSED QKPGHELDLD EADEEDLDEA LTTKDPTRAR
     KSFEDEEEEE ESAKLQEDQK VKEKEDKDKG DDGASGRSSP CLSTHSQASS LASGSVRMTS
     FAERKAQQRF GSNQDLRTSA SSSQRTTPDG SECSGPLSLP TSWRLKRDQS PCSPQGGRGD
     GGNNVLASEL VQLHMQLEEK RKAIEHQKKK MEVLSARQRQ KLGKAAFLHI VKKGKSDTLP
     HLLKPDHYSK EELNGDKGGS SKDDSCVDML RAAKETDSSA SPVPGAFEAV DRKGSRSPGP
     LLDEELDLNE CNRSIDMLND AIGSIQQQMM QLSLQQEQLM KQNVQSPPGV LSPSLTNDKP
     AVSEPKARAA VHFVEIGSGT PATGTAPTRK PPKLTSARGP RSKPSELKLA KEHGRQGLAS
     SRAITPTHSL ETLPHLRQFP GGRSPRADQP DASPRTPPAI GETNSGQDKP GRSATFRLHD
     ESNLRAVARN EPVTITTPEV SFDECLSSTP REGELNSSDG SGKENVPSEE VSRSKAPLIE
     VDLSDLKDPE ELEGEGQEST IEGDDGELKS GLGFFFKDEQ KAEDELAKKR AAFLVRQQKK
     AEEARLRKLQ LEAESEQKRE EARQKAEEDR MRKEEEKARR ELIKEQYLRR KQQELMEEQG
     LGSPAKPKTP KTKPKKAVHQ THRPKSAFSR EESSSDTFSS KCSSSTPDNL SSAQSGSSLS
     LASAATTEPD SVNSGGAGSQ RGESVESFPG LSRNASRNTE RDWDNGSTAS SITSMAEYTG
     PKLFKEPSSK SNKPIIFNAI THCCLAGKVN EAQKNTLLEE LEKVEAHHLM ILFRDGGCQF
     RGVYSYFPDT EEILKLTGTG PKSISKKMID KLYKYSSDRK QFTVIPAKTV SVSIDAITIH
     NHLWQAKRTT MPKKAGK
//
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