ID A0A3Q1GRW3_9TELE Unreviewed; 1545 AA.
AC A0A3Q1GRW3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Calmodulin regulated spectrin associated protein 1 {ECO:0000313|Ensembl:ENSAPOP00000033506.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000033506.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000033506.1}
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; ENSAPOT00000028413.1; ENSAPOP00000033506.1; ENSAPOG00000022146.1.
DR GeneTree; ENSGT00950000182975; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:UP000257200}.
FT DOMAIN 218..333
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1408..1542
FT /note="CKK"
FT /evidence="ECO:0000259|PROSITE:PS51508"
FT REGION 377..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 836..870
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 377..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 170560 MW; B99CF8828F5178AB CRC64;
MDVDLCAGGD STRRKVELSG VAEGTMDVVP LEMYDSARAK IAANLRWLFA KAYGIDHIPE
DLRDPFYTDQ YDQEHIKPPV IRLLLSCELY CRVCALILKT EQAASLQSHL SVIQALSRKG
IYVVESDDTP VTEGDLACMP IKMSAHMPMI DALMMAYTVE MISIEKVVAS VKRFSTFSAS
KELPFDLEDA MIFWINKVNM KMREITDREH KVKHHPLESP SHQKVRYRRE HASGRQLPFF
PLLEDLMRDV CDGAALLTVV HYYCPDLMKL EDICLKEVPS IADSLYNIQL LREFANEYLN
KSFYLTTEDM LYSPLVLKHN VMVFIAELFW WFETVKPEFV QPRDLQEFKD ARAMAHPKSS
RPSVPISNAT KRSFLVSPGA ADNQSSPEVC NSKGGPTFSP SHPLLPLRQR QQKHQGEDST
GLRNRSNSLT QMDGQQPRGS VVAWSDKRQR PLSTLSPYLL HSATDSDADM ASGDSVSLAR
SISKDSLASN VMNATPKHQA SAHQPSHAAM RRVNGHSLLG NANIEDEEEI LVAVARTDSP
VVPKRVDGTQ AAAPGGPKPS TDSKPAPDSF YLEPLMPAVL KTAKEKSVCL NKEEESGEVS
RSAGRGSLRR GDGSASAVRR KAPSNLNQTF TPPGEEIDST EEPPQDDAGF RPAVTSSVDP
SSREPAEGFY LHSDSEEPKS SQGLDAELED LDEEEEDLDE AVTTKDTNWP RKALNEEDEE
EESAKLQEDM NVKEHEDKDM NGGSGRSSPC LSTHSQASSM ASGSVRMTSF AERKAQQQRF
GSNHDLRSSA SSSQRTTPDG SESSGPLPSS WRLKRDQSPS SPLGGCNRTG DGSGGANVLA
SEIVQLRMQL EEKRRAIEHQ KKKMEVLSAR QRQKLGKAAF LHIVKKGGGK SDTLPNPLKA
DISKDDLNGE KGPSSKDDMC VETLRGEKEM EGTTPPGALG ADKKGNNGSF YVEEELDLNE
CSRSIELLNE AIGSIQQQMM QLSLQQEMLM KQNVQSPPGA APPPPTSDKN GESKAGATFH
YVEHLSGSST APTRKPPKLS SGRSSRSKPS ELKIAKEQSR QAARTLTPTQ SGSETLPHPR
QLAGGRSPRA EQPDSPRNPT AGETIDRPGA GHIRSATFRL QDEANMRLPT RVDLTSVAAP
EVSFDECLSS TLRESELNSS DGSGKENIPS EDAQRSKAHL IEVDLSDLKA PEEEDSAQDG
TTEGGDGEQK SVMGFFFKDE QKAEDELAKK RAAFLLKQQK KAEEARLRKQ QLEAESELKR
DEARRKAEED RLRKEEEKTR RELIKQEYLR RKQQEMFEEQ GLVKPKTPKP KQKHRPKSVF
REESSSDNFS KCSSTPDNLS NAQSGSSLSL ASAATNEADS VNSGGAGSQR CDSVESFPGS
RNNSRTAERD WDNGSTASSI TSMAEYTGPK LFKEPSAKSN KPIIHNAISH CCLAGKVNEP
QKNQILEELE KCESNHLMIL FRDGGCQFRA LYSYFPDTEE IQKLTGTGPK SISKKMIDKL
YKYSSDRKQF TVIPAKTVSV SVDALTIHNH LWQAKRSAVP KKSGK
//