ID G1KC05_ANOCA Unreviewed; 1881 AA.
AC G1KC05;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Coiled-coil domain containing 88A {ECO:0000313|Ensembl:ENSACAP00000003471.3};
GN Name=CCDC88A {ECO:0000313|Ensembl:ENSACAP00000003471.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000003471.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000003471.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000003471.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000003471.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_016846207.1; XM_016990718.1.
DR RefSeq; XP_016846208.1; XM_016990719.1.
DR STRING; 28377.ENSACAP00000003471; -.
DR Ensembl; ENSACAT00000003557.3; ENSACAP00000003471.3; ENSACAG00000003420.4.
DR GeneID; 100563386; -.
DR CTD; 55704; -.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000155559; -.
DR HOGENOM; CLU_001421_1_0_1; -.
DR InParanoid; G1KC05; -.
DR OrthoDB; 3091995at2759; -.
DR TreeFam; TF320231; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000003420; Expressed in forelimb bud and 12 other cell types or tissues.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0043422; F:protein kinase B binding; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0072660; P:maintenance of protein location in plasma membrane; IEA:Ensembl.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR043936; HOOK_N.
DR PANTHER; PTHR18947:SF30; GIRDIN; 1.
DR PANTHER; PTHR18947; HOOK PROTEINS; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR SUPFAM; SSF116907; Hook domain; 1.
DR PROSITE; PS50021; CH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646}.
FT DOMAIN 12..132
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 1013..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 245..424
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1356..1383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1416..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1843..1866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1881 AA; 216701 MW; D6A56C1EFEE56608 CRC64;
MENEIFTPFL EVFISSPLVT WVKTFGTLAG GRATHLEEYV ALVDGVFLNE VMLQINPKAA
SQRVNKKVNN DASLRIQNLS ILVRQIKSYY QETLQQLIMM PLPNVLIIGK SPFSEQGTEE
VKKLLLLLLG CAVQCQKKEE FIEKIQSLNF DIRAAVAAHI QEVTHNQENV FDLQWMDDNS
LSQDCIEPLL KNMALHLKRL IDERDEHSET IVELSEERDS LHFLPHASAA QSPCGSPGMK
RTESRQHLSV ELADAKAKIR RLRQELEEKT EQLLDCKQEL EQIEAEVKRL QQENMNLLSD
ARSARVYRDE LDALREKAIR VDKLESEVSR YKERLHDIEF YKARVEELKE DNQVLLETKT
MLEDQLEGTR ARSDKLHELE KENLQLKAKL HDMETERDMD RKKIEELMEE NMTLEMAQKQ
SMDESLHLGW ELEQINRSSE LSEVAPRKSL GHEVNELTSS RLLKLEMENQ SLLKTVEELQ
KMVGSAEGSN SKILKMEKEN QRLSKKLEGL ENELTEEKQS LQNSQNLSKD LMKEKAQLEK
TIETLRENSE RQIKILEQEN EHLNQTVASL RQRSQIGAEA RVKDIEKENK ILHESIKETS
SKLNKIEFEK KQMKKELEHH KEKGERADEL EKEVHHLEKE NEVLQKKVTN LRITCEKIDS
LEQENSSLDA ENRKLKKTLD GLKNLSFQLE SLEKENAQLD EENLELRRTV ESLKSTNIKI
AQLELENKEL ESEKGQLQKS LELMKTSFRK TERLEVSYQG LDTENQRLQK ALENSNKKIQ
HLESELQDLE TENQTLQKNL EELKISSKRL EKLEKENKLL EQETSQLEKD KKQLEKENKR
LRQQADITDN TLEENNVKIV HLETENRSLI KEIGICKESS IRLKEIEKEN KELVKRATID
KKTLVTLRED LVNEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD DSKYKLLESR
LESTLKKSLE IKEEKIAALE ARLEESTNLN QQLRQELKTV KKNYEALKQR QEEEKMVQNC
SSRSGEDGQS VNKWERESQE TTRELLKVKD RLIEVERNNA TLQAEKQALK TQLKQLETQN
SNVQAQILSL QRQTVSLQEQ NATLQTQNAK LQVENSAINS QSTSLMNQNA QLQIQQSTLE
NEKESIIKEQ EELKSQYDSL IKDHEKLEQL HERQAGEYES LISKHGSLKS AHKNLEVEHK
DLEDRYNQLL KQKVQLEELE KVLKTEQEKM LQQNKTHETV AADYKKLCEE NSRLNHTYTQ
LLKENEVLQV DHKNLKTLLN NSKLEQTRLE AEFSKLKEQY QQLDITYTKL NNQCELLSQL
KGNLEEENRH LLDHIQTLML QNKTLIESKD LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ
YKFYEPSPPR RRGNWITLKM RKLIKSKKEV NRERLKSLTM TPTRSESSEG FLQLPHQDSQ
DSSSVGSNSL EDGHTMGTKK SSMVALKRLP FLRNRPKEKD KMKAFYRRSM SMNDLMQSMV
LAGGQWTGSS EHLEGPDDLR TGKRRKELGS MAFSTTSINF ATVNSAAGLR SKQLLNNKDA
TSFEDVSPQG ISDDSSTGSR VHASRPASLD SGRTSTSNSN NNASLHEVKA GAVNKYQSRP
QSHSSGEFSL LHDHEAWSSS SSSPIQYLKN QTKSSPMLHH KMSEMLDRQG TRRIKTDSPG
SEVVTLQQFL EESNTVTSTE IKSSSQDNLL DEVMKIFSEN AELAGRQKLR KQSSGSSGIA
RSQSVKNTID SSGGKLVKQE HFGKLTSRRM EDPSSSNSSK TLTAGTKGRA KSVKENVQSQ
RQSKDCNPYA TLPRASSVIS TAEGTTRRTS IHDFLSKDTR QPVSIDPAPS TADRSVASVS
NVEAKPENRN SKSRSREQQS S
//
