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Database: UniProt
Entry: A0A1A6HXC0_NEOLE
LinkDB: A0A1A6HXC0_NEOLE
Original site: A0A1A6HXC0_NEOLE 
ID   A0A1A6HXC0_NEOLE        Unreviewed;       636 AA.
AC   A0A1A6HXC0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=A6R68_22891 {ECO:0000313|EMBL:OBS83113.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS83113.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS83113.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS83113.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS83113.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:OBS83113.1}.
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DR   EMBL; LZPO01007959; OBS83113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A6HXC0; -.
DR   STRING; 56216.A0A1A6HXC0; -.
DR   Proteomes; UP000092124; Unassembled WGS sequence.
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; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF130; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 15; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 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.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00068};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        595..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..341
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          348..435
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        407..427
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   NON_TER         636
FT                   /evidence="ECO:0000313|EMBL:OBS83113.1"
SQ   SEQUENCE   636 AA;  68406 MW;  7E519FDD0546FBAA CRC64;
     MFWDPAGGTE EPQQAKPERA LTGSLERQVV QDSPPVSLAE LLQENCCYRG EVQGHPGSWV
     SLCTCSGIRG LVVLSPERSY TLELGPGDLQ GPLIVSRIQD LLLPGHTCAP SWHALVPTQA
     GPNLLLGQHH IRRLKRDVVT ETKIVELVIV ADNSEVRKYP DFQQLLNRTL EVALLLDTPL
     NVRVALVGLE AWTQHDLIEM SSNPAVLLDN FLRWRRTDLL PRLPHDSAQL VTGTSFSGPM
     VGMAIQNSIC SPDFSGGVNM DHSTSILGVA SSMAHELGHS LGLDHDSPGS SCPCPGPAPA
     KSCIMEASTD FLPGLNFSNC SRQALEKALL EGLGSCLFER LPSLAPMSSL CGNMFVDPGE
     QCDCGFPDEC TDPCCDYFTC QLRPGAQCAS DGPCCQNCKL HPAGWQCRPR RDDCDLPEFC
     PGDSSQCPPD LRLGDGEPCA SGQAVCVHGR CASYAQQCQS LWGPGAQPAA PLCLQTANTR
     GNAFGSCGRS PNGSYVPCTP GDAICGQLQC QWHRSQPLLG SVQELRSEVL EANGMQLNCS
     WVHLDLGNDV AQPLLALPGT ACGPGLVCDS SRHCHCEEGW APPDCMTQLR ATSSLTTGLL
     LSLLLLLVLV VLGASYWHRA RLHQRLCQLK GSSCQY
//
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