ID G1PTS9_MYOLU Unreviewed; 1876 AA.
AC G1PTS9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Coiled-coil domain containing 88A {ECO:0000313|Ensembl:ENSMLUP00000014651.2};
GN Name=CCDC88A {ECO:0000313|Ensembl:ENSMLUP00000014651.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000014651.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000014651.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000014651.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAPE02005066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02005067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 59463.ENSMLUP00000014651; -.
DR Ensembl; ENSMLUT00000016083.2; ENSMLUP00000014651.2; ENSMLUG00000016070.2.
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000155559; -.
DR HOGENOM; CLU_001421_1_0_1; -.
DR InParanoid; G1PTS9; -.
DR OMA; AVATHIQ; -.
DR TreeFam; TF320231; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
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: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: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:0030705; P:cytoskeleton-dependent intracellular transport; IEA:InterPro.
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 CDD; cd22229; HkD_Girdin; 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:UP000001074}.
FT DOMAIN 12..132
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 816..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..425
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1127..1154
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1183..1385
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1418..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1876 AA; 216598 MW; C8C27505785ECAB4 CRC64;
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ VMLHINPKSE
SQRVNKKVNN DASLRIHNLS ILVRQIKCYY QETLQQLIMM SLPNILIIGK TPFCEQGTEE
VKKLLLLLLG CAVQCQKKEE FIERIQGLDF DTKAAVAAHI QEVTHNQENV FDLQWMEVTD
MSQEEIEPLL KNMVLHLKRL IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM
KRTESRQHLS VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS
DARSARMYRD ELDALREKAI RVDKLESEVS RYKERLHDIE FYKARVEELK EDNQVLLETK
TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM DRKKIEELME ENMTLEMAQK
QSMDESLHLG WELEQISRTS ELSEAPQKSL GHEVSELTSS RLLKLEMENQ SLTKTVEELR
STMDSAEGNT SKILKIEKEN QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK
TIETLRENSE RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS
SKLSKIEFEK RQIRKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN LKITCEKIEA
LEQENSELER ENRKFKKRLD SFKNLTFQLE SLEKENSQLD EENLELRRNV ESLKCASMKM
AQLQLENKEL ESEKEQLKKG LELMKASFKK SERLEVSYQG LDTENQRLQK ALENSNKKIQ
QLESELQDLE MENQTLQKNL EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR
LRQQAEIKDT TLEENNVKIG NLEKENKTLF KEIGIYKESC IRLKELEKEN KELVKRATID
IKTLVTLREN KDLVSEKLKT QQMNNDLEKL THELEKIGLN KERLLHDEQS TDDSRYKLLE
SKLESTLKKS LEIKEEKIAA LEARLEESTN YNQQLRQELK TVKKNYEALK QRQDEERMVQ
SPPSASSEDN KWERESQETT RELLKVKDRL IEVERNNATL QAEKQALKTQ LKQLETQNNN
LQAQILALQR QTVSLQEQNT TLQTQNAKLQ VENSTLNSQS TSLMNQNAQL LIQQSSLENE
NESVIKERED LKSLYDSLVK DHEKLELLHE RQASEYESLI AKHGTLKSAH KNLEVEHKDL
EDRYNQLLKQ KGQLEDLEKT LKVEQEKMLL ENKNHETVAA EYKKLCGEND RLNHTYNQLL
KETEVLQTDH KNLKSLLNNS KLEQTRLEAE FSKLKEQYQQ LDITSTKLNN QCELLSQLKG
NLEEENRHLL DQIQTLMLQN RTLLEQNMES KDLFHVEQRQ YIDKLNELRR QKEKLEEKIM
DQYKFYEPSP PRRRGNWITL KMRKLIKSKK DINRERQKSL TLTPTRSDSG EGFLQLPHQD
SQDSSSVGSN SLEDGQTLGT KKSSMVALKR LPFLRNRPKD KDKMKACYRR SMSMNDLVQS
MVLAGGQWTG STENLEVPDD ISTGKRRKEL GAMAFSTTAI NFSTVNSSTG FRSKQLVNNK
DATSFEDISP QGISDDSSTG SRVHASRPAS LDSGRTSTSN SNNNASLHEV KEAGAVTIQS
RPQSHSSGEF SLLHDHEAWS SSGSSPVQYL KRQTRSSPVL QHKMPETESR AHHKVKTGSP
GSEVVTLQQF LEESNKLTSI QIKSSSQDNL LDEVMKSLSV SSDFLGKSKP VSCGLARSVS
GKSPGDFYDR RTTKPEQFVR PGPQKTEDTY FVSSPGKPTP GTQGKIKLVK ESSLSRQSKD
SNPYATLPRA SSVISTAEGT TRRTSIHDFL TKDSRLPMSV DPSPAVADSH ITAASNVDKV
QESRNSKSRS REQQSS
//
