ID G3STV6_LOXAF Unreviewed; 785 AA.
AC G3STV6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 78.
DE SubName: Full=Rabenosyn, RAB effector {ECO:0000313|Ensembl:ENSLAFP00000003524.3};
GN Name=RBSN {ECO:0000313|Ensembl:ENSLAFP00000003524.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003524.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000003524.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003524.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000003524.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003524.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR RefSeq; XP_003409791.1; XM_003409743.2.
DR RefSeq; XP_010588242.1; XM_010589940.1.
DR RefSeq; XP_010588243.1; XM_010589941.1.
DR AlphaFoldDB; G3STV6; -.
DR STRING; 9785.ENSLAFP00000003524; -.
DR Ensembl; ENSLAFT00000004226.3; ENSLAFP00000003524.3; ENSLAFG00000004227.3.
DR GeneID; 100654020; -.
DR KEGG; lav:100654020; -.
DR CTD; 64145; -.
DR eggNOG; KOG1842; Eukaryota.
DR GeneTree; ENSGT00390000007159; -.
DR HOGENOM; CLU_020798_2_0_1; -.
DR InParanoid; G3STV6; -.
DR OMA; CNDCSKF; -.
DR OrthoDB; 1441111at2759; -.
DR TreeFam; TF106125; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0034498; P:early endosome to Golgi transport; IEA:Ensembl.
DR GO; GO:0090160; P:Golgi to lysosome transport; IEA:Ensembl.
DR GO; GO:1903358; P:regulation of Golgi organization; IEA:Ensembl.
DR CDD; cd15716; FYVE_RBNS5; 1.
DR Gene3D; 4.10.860.20; Rabenosyn, Rab binding domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR021565; Rbsn_Rab-bd.
DR InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13510; FYVE-FINGER-CONTAINING RAB5 EFFECTOR PROTEIN RABENOSYN-5-RELATED; 1.
DR PANTHER; PTHR13510:SF44; RABENOSYN-5; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF16601; NPF; 1.
DR Pfam; PF11464; Rbsn; 2.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF140125; Rabenosyn-5 Rab-binding domain-like; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 14..42
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 157..260
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 207..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 207..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 88979 MW; 736EC9EE63CA29EB CRC64;
MASLDDPGDV REGFLCPLCL KDLQSFYQLQ AHYEEEHSGE DRDVRGQIKS LVQKAKKAKN
RLLKREGDDR AESGTQGYES FSYGGVDPYM WEPQELGAMR SHLSDFKKHR AARIDHYVVE
VNKLIIRLEK LTAFDRTNAE SAKIRAIEKS VVPWVNDQDV PFCPDCGNKF TLRNRRHHCR
LCGSIMCKKC MEFVNLPLAN KLTSASKDSL STHTSPSQSP TSVHGSRRGS VSSMSSVSSV
LDEKDDDRIR CCTHCKDTLL KREQQIDEKE HTPDIVKLYE KLRLYMEKVD RKAPEYIRMA
AALNAGETTY SLEHANDLRV EVQKAYELID ALSKKILTLG LNQDPPAHPN TLRLQRMVRY
SATLFVQEKL LGLMSLPTKE QFEELKKKRK QEMEKKRILE RQAALESQRR LVERHGDLAS
RTTNGEVASL HRGPAPLRKA EGWLPLSGGQ GHGEDSDPLL QQIHNITSFI RQAKAAGRTD
EMRTLQENLR QLQDEYDQQQ TEKAIELSRR QAEEEDLQRE QLQMLQEREW EREREQFQAT
SLHTRTQFLD IQEVRPFQLE PGREPHTHPT YALDPGSPLV KSSVAPKTSS PCSAGEPIRM
CSGPPALSQE FFLRSTMSQQ NEVPALNPFD EEDLSSPAEE GTGSSPATEV SFGPSARIPK
EYNPFEEEEE EEEAVAGNPF TTPDGPVPNP FDEEGEHHSQ RPSSPPVPGN PFEEPASTNP
FEMDSDSGPE GEEPIEEELL LQQIDNIKAY IFDAKQCGRL DEVEVLTENL RELKRTLAKQ
KGGTD
//