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Database: UniProt
Entry: K7FJI8_PELSI
LinkDB: K7FJI8_PELSI
Original site: K7FJI8_PELSI 
ID   K7FJI8_PELSI            Unreviewed;      1608 AA.
AC   K7FJI8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSPSIP00000008198.1};
GN   Name=CAMSAP1 {ECO:0000313|Ensembl:ENSPSIP00000008198.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000008198.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000008198.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AGCU01070038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01070039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01070040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01070041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01070042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006120849.1; XM_006120787.2.
DR   STRING; 13735.ENSPSIP00000008198; -.
DR   Ensembl; ENSPSIT00000008241.1; ENSPSIP00000008198.1; ENSPSIG00000007403.1.
DR   GeneID; 102444603; -.
DR   CTD; 157922; -.
DR   eggNOG; KOG3654; Eukaryota.
DR   GeneTree; ENSGT00950000182975; -.
DR   HOGENOM; CLU_004833_1_0_1; -.
DR   OMA; EANHYII; -.
DR   OrthoDB; 2918432at2759; -.
DR   TreeFam; TF315529; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0036449; C:microtubule minus-end; IEA:Ensembl.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0051011; F:microtubule minus-end binding; IEA:Ensembl.
DR   GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0031113; P:regulation of microtubule polymerization; IEA:Ensembl.
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:UP000007267}.
FT   DOMAIN          217..332
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1469..1603
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          354..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1248..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1301..1432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          878..908
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1027..1054
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        430..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..793
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1079
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1113..1127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1301..1356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1388..1430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1608 AA;  180213 MW;  AB246657842BA328 CRC64;
     MVDVDVCAGG DSTRRKMDAL TDSAVEIVPL ELYDSARAKI AANLQWICAK AYGIDNIPEE
     LKDPFYIDQY EQEHIKPPVI KLLLSSELYC RVCSLILKGD QVAALQGHQS VIQALSRKGI
     YVMESDDTPV SESDLACAPI KMSSHMAMID SLMMAYTVEM ISIEKVVASV KRFSTFSASK
     ELPYDLEDAM VFWINKVNLK MREITEKEVK LKQQLLESPG HQKVRYRRDH LSSRQLPYFP
     LLEDLMKDGS DGAALLAVIH YYCPEQMKLD DICLKEVTSI ADSLYNIQLL REFSNEYLNK
     CFYLTLEDML YAPLVLKPNV MVFIAELFWW FENVKPDFVQ PRDIQEIKDA KTVLQQKSSR
     PPVPISNATK RSFMASPAST SPADLQPSIQ LPQEACNRYY LHPEESDYLG KGSPAFSPSH
     PLLPLRQKQQ KSLQEEDCSS HRHRSNSLTR VDGQPRGSVL AWPEKKPRPL SQPTPFALHH
     ATSSDVDPGS GDSISLARSI SKDSLASNIV TLTPKHPSHP SSMKTNGKTL LNNVEIEDED
     EELIAIIRSD EIPDHDDLEL QSVSSRAPSL VAAAWSSKPQ SEAIESKADS FYLEPLMPAV
     LKPAKEKQIT NKEDECGEGK QRGFITKRLN EGHLPMVRKK ANSSHADHDI NRTFTPISSS
     DFTAVADPCT ADSVTLSEAG FEAPRPSASS SLEPSSQEQS TGGFFLHTAK VEDVTRKVSV
     SYVKSTNSHI PSPTWTVVRQ DSDSDLDTDV AEQDLVVVDD RPVVSKYIGE EESAKLQEDM
     KVKEHEDKDD ASGRSSPCLS TISQVSSVSM TSGSVRMTNF AERKLQRLNS YETKSSTSSS
     QKTTPDGSES CPAPLTTWKQ KREQSPTRQN KDNVTLLASE LVQLHMQLEE KRRAIEAQKK
     KMEALSARQR LKLGKAAFLH VVKKGKAVDV PQPLKPEHFA KEYSRNSGED LDDVSLSSKS
     EEFLVKEEER EEMFYDSQEV SKMKMQENLA LVELHKPKEC AAMHEIEKSK IISAALLEDN
     GAEVVDINEC DLSIEKLNET ISTLQQAILK ISHQQELLMK SPTVPSPSIR NNSQDQKVKP
     SIHFVEPLSP TGMSSLRKPP RLGQGRGPRS GRPAELRVAK DRHQNSTRIK TPTQSVETLP
     HLRPFPANNP CRTPTEASFE NSPDHGSGSQ DKFFFDSYRR HDESNQRAFV LSTSKDANII
     SEMSKDMNSS LKEEGLNSSD GSGKENVPVD EPLKNKVNLI EVDLSDLKAP DEEGEIESQD
     SSTDLINEGD QKSGVGFFFK DEHKAEDELA KKRAAFLLKQ QRKAEEARIR KQQLEAEVEQ
     KRDEARRKAE EDRIRKEEEK ARRELIKQEY LRKKQQQILE EQGLGKPKSK PKKPRPKSVH
     REESYSDSGT KCSSTPDNLS SAQSGSSLSL ASAATTEPES IHSGGTPSQR VESMEFLPIL
     SRNPSRNTER DWENASTASS IASVAEYTGP KLFKEPSSKS NKPIIHNAIS HCCLAGKVNE
     PHKNSILEEL EKCDANHYII LFRDAGCQFR ALYCYYPDTE EIYKLTGTGP KSINKKMIDK
     LYKYSSDRKQ FNLIPAKTMS VSVDALTIHN YLWQAKRPAV PKKTQTRK
//
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