ID A0A1V4JQJ6_PATFA Unreviewed; 1123 AA.
AC A0A1V4JQJ6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein CASC3 {ECO:0000256|ARBA:ARBA00019964};
GN Name=CASC3 {ECO:0000313|EMBL:OPJ74468.1};
GN ORFNames=AV530_001323 {ECO:0000313|EMBL:OPJ74468.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ74468.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ74468.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ74468.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ74468.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CASC3 family.
CC {ECO:0000256|ARBA:ARBA00009548}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ74468.1}.
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DR EMBL; LSYS01006700; OPJ74468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JQJ6; -.
DR STRING; 372326.A0A1V4JQJ6; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0035145; C:exon-exon junction complex; IEA:InterPro.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00155; RasGEF; 1.
DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR InterPro; IPR018545; Btz_dom.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13434; PROTEIN CASC3; 1.
DR PANTHER; PTHR13434:SF0; PROTEIN CASC3; 1.
DR Pfam; PF09405; Btz; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SMART; SM01044; Btz; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-ProRule:PRU00168};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 885..1121
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT REGION 1..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..35
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 126865 MW; B153DBDCC10DA91C CRC64;
MLGRESEDGI EGDAVLSDYE SAEDSEAEEE DYSEEESAKV ELKHDSNDSC ESAAKAEKGD
EKPDSRGAVT GERQSGDGQE STEPVENKVG KKVPKHLDDD EDRKNPAYIP RKGLFFEHDL
RGQTQEEEVR PKGRQRKLWK DEGRWEHDKF REDEQAPKTR QELIALYGYD IRSAHNPDDI
KPRRMRKPRF GSPPQRDPNW SNERPNKPPR HQGADSTSAP PRTFTNRSSA GTGRMPPPRN
YPRMGGYKET RPGYRASEAS VQHLSRNSEQ AKQESSYRAK RVEQTPPRDK SPEMEAAHVH
GSPVKEEVAL ENQTAAADAA QPPPDRPIEK KSYSRARRTR IKAGDAGKLA DEAPASEGLN
PAPPKPAEAE TCPPPAKSSN WESPVESNLD GLEQEMTQMN LTEQNWTPGQ SQFLQPRELR
GIPNHMHVGT GPPPQFNRME EMAVQGGRVK RYSSQRQRAP VPEPAPPMHI SIMEGHYYDP
LQFQGPIYTH SENPAPLPPQ GMIVQPEMHL PHPGLHPHQT PAPMANPGLY PPPVSMPPGQ
PPPQQLLAPT YFSPPGVMNF GNPGYPYPPG ALPPPPPPHL YSNTQAQSQV YGGVTYYNTV
QQQVQPKPSP PRRTSQPVTI KPPPPEDSKE LLLDDIVLTH SLFLPTERFL QQLHQHFVLA
GGSPPAHWER GSGLQRKQAV LAVLLHFLET YKGLLQEEES AGKVIKELYL LIMKDTSLYN
ELEDEILKLH QLVETVELKV ADETPPPNKQ VKPLFRHFRR IDSCLQTRVA FRGSDEIFCR
VYMPDHSYVT IRSRLSASVQ DILASVTEKL QYSEEQSARE DALILVTMAS SGEKAVLQPS
EECVFTTLGI NSHLFACTRD TFDSLVPLPE EIQVVPGDTE IHRAEPEDIA NHLTAFHWEL
FRCIHELEFV DYVFHGERGR RETANLELLL QRCSEVQHWV GTELLLCESL GKRAHLLKKL
IKIAAICKQN QDMLSFYAII IGLNNAAISR LRLTWEKLPG KFKNLFRKFE NLTDPCRNHK
TYREVLAKMK PPLIPFLPLI LKDLTFLHEG SKTLLDGLVN VEKLHCIADK VRTIRKYRSR
PLCLELEASP SQLQTKAYVR QLRVIDNQNL LFELSYKLEP GSQ
//
