ID G3WDC9_SARHA Unreviewed; 787 AA.
AC G3WDC9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=ADAM metallopeptidase domain 12 {ECO:0000313|Ensembl:ENSSHAP00000013434.2};
GN Name=ADAM12 {ECO:0000313|Ensembl:ENSSHAP00000013434.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000013434.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000013434.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000013434.2}
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 AlphaFoldDB; G3WDC9; -.
DR Ensembl; ENSSHAT00000013545.2; ENSSHAP00000013434.2; ENSSHAG00000011484.2.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000155495; -.
DR HOGENOM; CLU_012714_7_0_1; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000007648; 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; IPR018358; Disintegrin_CS.
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; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF112; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 12; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
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 570..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..278
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 286..372
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 518..550
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 637..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 344..364
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 522..532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 540..549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 787 AA; 85112 MW; 051972ED6AA81FB0 CRC64;
LGHCYYHGHV QGHPDSIVSL STCSGLRGGG LHLWLCEPPR GSRAGSLPLR GPFAGLSVCP
PQGRSGRKRE TLKTAKYVEL VIVADNREFQ RQGKDVEKVK QRLIEIANHV DKFYRPLNIR
IVLVGVEVWN DIDKCSISQD PFTSLHEFLD WRKMKLLPRK PHDNAQLVSG VYFQGTTIGM
APIMSMCTAE QSGGVVMDHS DSPLGAAVTL AHELGHNLGM NHDTLERGCH CQAMTDKGGC
IMNPSTGYPF PVMFSSCSRR DVETSLEKGM GMCLFNLPDI KEAFGGQKCG NGYVEEGEEC
DCGEPDECTN PCCNATTCTL KPEAVCAHGL CCENCQLKAA GTACRASSNS CDLPEFCTGA
HPHCPANVYL HDGHRCHRVD GYCYNGICQT HEQQCVTLWG PGAKPAPGIC FERVNSAGDP
YGNCGKNSKS SFAKCEMRDA KCGKIQCQGG ASRPVIGTNA VSIETNIPLQ EGGKILCRGT
HVYLGDDLPD PGLVLAGTKC EEGKLCLNRR CQNVSVFGVH ECATKCHGRG VCNSNKNCHC
EADWAPPFCD RPGFGGSVDS GPMRQADKRG LALGILVTVF CLLAAGFVTY LKRKALIRLL
FTNKKTKTTI EKLRCVSPTR PAGVTEPNRT RAANLGQGLL RKPPHGDMPK ENCRRSPKYQ
NINISNPVKS LNPCPAGLLL PLPQGPSHQA VPARPLPANP AVRQAQGTHK PSPPQKPLPA
DPLSRAARLS ETSRKAPGPQ EAGHRLIPTR LVPSFPLIFP PSCQTALYIH GLVSSSKRPQ
SKKSSLK
//
