ID H9G3Y4_ANOCA Unreviewed; 483 AA.
AC H9G3Y4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000000541.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000000541.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000000541.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000000541.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000000541.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; H9G3Y4; -.
DR Ensembl; ENSACAT00000000560.3; ENSACAP00000000541.3; ENSACAG00000000645.3.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT01030000234669; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; H9G3Y4; -.
DR TreeFam; TF338674; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000000645; Expressed in adrenal gland and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 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; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_euk.
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; PTHR24103:SF691; B30.2_SPRY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
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; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Neurotoxin {ECO:0000256|ARBA:ARBA00022699};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Toxin {ECO:0000256|ARBA:ARBA00022699};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 29..70
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 92..133
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 289..483
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
SQ SEQUENCE 483 AA; 55708 MW; 34FCA201CFEEF643 CRC64;
SENKGLWSQE RKKATGVFAA MDLSYEWTCP ICLETFKNPV TIDCGHNFCQ ACLSQYWGSA
NRSSSCPQCR QMVPQRSFQP NRLLVSMIER WKKTGTCAKH WLPLNRFCKE DETLLCSVCE
RSKEHLDHVA VSWEDVAPEY KEQIEASMKS LQKRRMLVLK QMSIEAHGKK ECLKQIELEN
QKISSAFDQM QNFLKEKKCF WLGQLQDLES NVKEKHEKNI STLSKEVLYL GNLIAVMNEK
FQQPGDEFLQ RSHCVCLSFQ FAVLPSMQHG LQNKWRTKVT IYLETTFGML RNFSPHNGRK
ITAQLSMDVT LDPNTANAFL ILSGDLKSVI CGTEEQKVPN VPERFDWELC VLGCDRFTSG
NSWWEVEVKK EGEMWVLGVA KETIRRKRSF IPNPSEDTWA IGKPSGKSFS SNELWAFTSP
KPTLLILRHS PRKILVSLNY EEGRVEFFDA DSDELIFTFL AASFRGETIR PFFWVTPGVW
LKC
//
