ID A0A3Q1N120_BOVIN Unreviewed; 1179 AA.
AC A0A3Q1N120;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=MCF.2 cell line derived transforming sequence like {ECO:0000313|Ensembl:ENSBTAP00000062589.1};
GN Name=MCF2L {ECO:0000313|Ensembl:ENSBTAP00000062589.1,
GN ECO:0000313|VGNC:VGNC:31302};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000062589.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000062589.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000062589.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000062589.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000062589.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A3Q1N120; -.
DR Ensembl; ENSBTAT00000084550.1; ENSBTAP00000062589.1; ENSBTAG00000017289.5.
DR VEuPathDB; HostDB:ENSBTAG00000017289; -.
DR VGNC; VGNC:31302; MCF2L.
DR GeneTree; ENSGT00940000157874; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000017289; Expressed in cerebellum and 98 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1N120; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01227; PH_Dbs; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 1.20.58.60; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR035534; DBS_PH.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF115; GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00435; Spectrin; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1179
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018769208"
FT DOMAIN 20..192
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 599..779
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 797..913
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 523..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 132470 MW; BE223D5719FF351A CRC64;
MTLSLLSLLS RDLSTLWLLL KTRTDEIMHH DISPLCAADI RDQLQKRFAY LSGGRGQDGS
PVITFPDYPA FGDVPDQDFQ NVMTYLTSIP SLQDAGIGFI LVIDRRQDRW TSVKASILRI
AASFPANLQL VLVLRPTGFF QRTLSDLAFR FNRDDFKMKV PVIMLSSVPE LHGYIDKSQL
TEDLGGTLAY CHSRWLRHRT AIESFALLVK QTAQMLQTFG TELAETELPN DVQSTSSVLL
AHTEKKDRAK EDMRLALVEG RRVLESIHEP LARSPDQSPN QDQLDSQSTV HRLLAQLNET
EAAFDEFWAK HQQKLEQCLQ LRHFEQDFRE VKSALDVLAQ KVTTFTDVGN SLAHVQHLLK
DLTSFEEKSS AAVQRARTLS QEGERLIEHK HYAVDSIRPK CHELRHLCDQ FAADVERRRG
LLGKSLELHG LLEASMKWCD EGIYLLASQP VDKCQSQDGA EAALQELERF LETGAENKIQ
ELSKIFQDYE PILTKDLLEH VQRVFQKQES VEEMFHRRQA SLKKLAAKQT RPVQPVAPRP
EALTKSPCPS PGIRRGSENH SSEGSALRRG PYRRAKSEVS EGRQGRGGST GDEESLAVLR
RHVMKELLDT ERVYVEELLC VLEGYAAEMD NPLMTHLIST GLQNKKDILF GNMEEIYHFH
NRIFLRELEN YTDCPELVGR CFLERMEEFQ IYEKYCQNKP RSESLWRQCS DCPFFQECQK
KLDHKLSLDS YLLKPVQRIT KYQLLLKEML KYSKSCEGAE DLQEALSSIL GILKAVNDSM
HLIAITGYEG NLSDLGRLLM QGSFSVWTDH KRGHAKVKDL ARFKPMQRHL FLHEKAVLFC
KRREENGEGY EKAPSYSYKQ SLNMTAVGIT ENVKGDAKKF EIWYNAREEV YIIQAPTPEI
KAAWVSEIRK VLTSQLQACR EASQHRALEQ SQSLPLPTPA GTSPSKASTR NIKKLEERKT
DPLSLEGYGG PTPQQRAPEK GKDDAVTSST SESSALSKKR FTLQSFAALK AQKASPTSPD
KKAKRHQVKS DPTPFGLRGW SKTSHPSETP EDNDGWSSTE EPVNSSDAEE EGRAGPGKLV
PGRYTVTRLD EKGVSDVLAL RSGDEVELVQ EGDEGLWCVR NLSSGVEGWV PAHSLSTLLC
QGGPVGCLSS PESSAGSAVL SPSSSCSESC TAALADLQG
//
