ID   A0A2K6N783_RHIRO        Unreviewed;       787 AA.
AC   A0A2K6N783;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=ADAM metallopeptidase domain 33 {ECO:0000313|Ensembl:ENSRROP00000000137.1};
GN   Name=ADAM33 {ECO:0000313|Ensembl:ENSRROP00000000137.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000000137.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000000137.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; A0A2K6N783; -.
DR   Ensembl; ENSRROT00000000337.1; ENSRROP00000000137.1; ENSRROG00000000110.1.
DR   GeneTree; ENSGT00940000158971; -.
DR   Proteomes; UP000233200; Unplaced.
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   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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00068}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
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..787
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014381919"
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   REGION          720..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..734
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"
SQ   SEQUENCE   787 AA;  84937 MW;  758B8443C2E6889D CRC64;
     MGWRPGRARG SPFLLLLLLL LLWPVPGAGV LQGHIPGQPV TPHWVLDGRP WRAVCLEELV
     LKPDMGLVAL EAEGQELLLE LEKNHRLLAP GYIETHYGPD GRPVVLAPNH KDHCYYHGRV
     RGFPNSWVVL CTCSGMSGLI TLSSNASYYL RPWPPRGSKD FSTHKIFRME QLLTWKGACG
     HRDPGDKAGM ASLPGAPQSR DRREARRTWR YLELYIVADH TLFLTQQRNL NHTKQRLLEV
     ANYVDQLLRT LDIQVVLTGL EVWTERDLSR VTQDANATLW AFLQWRRRLW AQRPHDSAQL
     LTGRAFQGAT VGLAPVEGMC RAESSGGVST DHSELPIGAA ATMAHEIGHS LGLSHDLDGC
     CVEAAAESGG CVMAAATGHP FPRVFSPCSR RQLRAFFRKG GGACLSNAPD PGLPVLPARC
     GNGFVEAGEE CDCGSGQECR DLCCFAHNCS LRPGAQCAHG DCCMHCLLKP AGALCRQAMG
     DCDLPEFCTG ISSHCPPDVY LLDGSPCARG SGYCWDGACP TLEQQCQQLW GPGSHPAPEA
     CFQVVNSAGD AHGNCGQDSK GHFLPCAGRD ALCGKLQCQG GKPSLLIQHM VPVDSTVHLD
     GHEVTCRGAL ALPGAQLDLL GLGMVEPGTQ CGPRMVCNSN HNCHCAPGWA PPFCDNPGFG
     GSTDSGPVQP ENRDTFLLAM LLSVLLPLLP GAGLAWCCYR LPGAHLQRCS WGCRRDPACS
     GPKDGPHRDH PLGGVHPMEL GPTATGQPWA LGPENSHEPS SHPEKPVPAV PPDPQADQVQ
     MPRSCLW
//