ID G1R7V9_NOMLE Unreviewed; 842 AA.
AC G1R7V9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=ADAM metallopeptidase domain 33 {ECO:0000313|Ensembl:ENSNLEP00000009288.2};
GN Name=ADAM33 {ECO:0000313|Ensembl:ENSNLEP00000009288.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000009288.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000009288.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000009288.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; ADFV01104460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1R7V9; -.
DR STRING; 61853.ENSNLEP00000009288; -.
DR Ensembl; ENSNLET00000009733.2; ENSNLEP00000009288.2; ENSNLEG00000007629.2.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000158971; -.
DR HOGENOM; CLU_012714_7_0_1; -.
DR InParanoid; G1R7V9; -.
DR OMA; MGAQCAH; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000001073; Chromosome 13.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF38; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 33; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..842
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014181264"
FT DOMAIN 210..409
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 417..503
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 649..681
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 746..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 475..495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 653..663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 671..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 842 AA; 90649 MW; C48C2E3526ACF89B CRC64;
YGLEALETRG TRLLLLLLLL LLWPVPSAGV LQGHIPGQPV TPHWVLDGRP WHAVSLEEPV
PKPDVGLVAL EAEGQELLLE LEKNHRLLAP GYIETHYGPD GQPVVLAPNH TDHCHYQGRV
RGFPDSWVVL CTCSGMSGLI TLSSNASYYL RPWPSQGSKD FSTHKIFRMQ QLLTWKGACG
HRDPGDKAGM TSLPGAPQSR DRREARRTRK YLELYIVADH ALFLTRHRNL NYTKQRLLEV
ANYVDQLLRT LDIQVVLTGL EVWTERDRSR VTQDANATLW AFLQWRRGLW AQRPHDSAQL
LTGRAFQGAT VGLAPVEGMC RAESSGGVST DHSELPIGAA ATMAHEIGHS LGLSHDPDGC
CVEAAAESGG CVMAAATGHP FPRVFSACSR RQLRAFFRKG GGACLSNAPD PGLPVLPALC
GNGFVEAGEE CDCGSGQECR DLCCFAHNCS LRPGAQCAHG DCCTHCLLKP AGALCRQAMG
DCDLPEFCTG TSSHCPPDVY LLDGSPCARG SGYCWDGACP TLEQQCQQLW GPGSHPAPEA
CFQVVNSAGD AHGNCGQDSE GHFLPCAGRD ALCGKLQCQG GKPSLLAPHM VPVDSIVHLD
GHEVTCRGAL ALPSAQLDLL GLGLVEPGTQ CGPRMVCQSR RCRKTAFQEL QRCLTACHSH
GVCNSNHNCH CAPGWAPPFC DKPGFGGSMD SGPVQAENHD TFLLAMLLSV LLPLLPGAGL
AWCCYRLPGA HLQRCSWGCR RDPACSGPKD GPHRDHPLGG DHPMELGPTA TGQPWPLDPE
NSHEPSSHPE KPLPAVSPDP QGRQGPGFKV SPSHRPPSHL SHPSVCCPQS GFWAQVIMEM
SL
//
