ID V8P5N2_OPHHA Unreviewed; 623 AA.
AC V8P5N2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=E3 ubiquitin/ISG15 ligase TRIM25 {ECO:0000313|EMBL:ETE69192.1};
DE Flags: Fragment;
GN Name=Trim25 {ECO:0000313|EMBL:ETE69192.1};
GN ORFNames=L345_05008 {ECO:0000313|EMBL:ETE69192.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE69192.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE69192.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE69192.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Neurotoxin that produces dose-dependent hypolocomotion and
CC hyperalgesia in mice. May directly act on the central nervous system,
CC as it is 6500-fold more potent when administered
CC intracerebroventricularly than intraperitoneal.
CC {ECO:0000256|ARBA:ARBA00034460}.
CC -!- SIMILARITY: Belongs to the ohanin/vespryn family.
CC {ECO:0000256|ARBA:ARBA00009651}.
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:ETE69192.1}.
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DR EMBL; AZIM01000824; ETE69192.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P5N2; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR CDD; cd19769; Bbox2_TRIM16-like; 1.
DR CDD; cd16597; RING-HC_TRIM25_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR PANTHER; PTHR25465:SF40; E3 UBIQUITIN_ISG15 LIGASE TRIM25; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Ligase {ECO:0000313|EMBL:ETE69192.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Toxin {ECO:0000256|ARBA:ARBA00022699};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 19..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 435..623
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 444..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE69192.1"
SQ SEQUENCE 623 AA; 70882 MW; B33207BE26F60AAA CRC64;
MASSVEALSM FGLEEELTCS ICLCLFQTPV TTPCGHNFCL PCLEMTWMEF EEKFSCPQCR
ASFETRPELK KNTVLCKVVE QFQISQDGLS QGCTLLFALF RLSSPTKPRP SSPVPCDNCL
VVDATKTCLT CMASFCQEHL GPHLESPAFK GHQLVPPVKE LQQKKCQAHT KLLEFFCHEH
RVPICCFCLL SHKTCSTTPL KEAKEAKELQ LKKRLTELSA LNDKTAKSLE QVRTQQKQLS
ANLEDPEFQN RLTLPPLTSS GLSPSHLSAV AEIETCGSTI SFSAPCSPEV ERSHNLFKVM
WHFSKSFFIL MILSFQNTTS WKLDLLKSEF REILALIHEE EQNSWKKIKS EEKRVLDKFE
FVHTVLGKKK NEIQMERGEI EVILAEMDDI TFLKRATKRR QISFSDVFVP KIELDQNVLG
AVYQKACNLK EVTKRFLNIT QEEKIKEQRS RPAKRSESPK PRARSSGKAE PKSETTTLDT
FLTKPREEIL KLLSFQCFKK GIHYWEVDLE NNNFCAVGIC YGSIPRRGPE SRLGRNSSSW
CIEWVNNKVS AWHNGKDTAL PTSKATKIGV LLNYDGGFVI FFGVTEKKIF TLYKFKIEFT
EAVYSAFWVF SNGATISICQ LKS
//
