ID W5PHD0_SHEEP Unreviewed; 752 AA.
AC W5PHD0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=ADAM metallopeptidase domain 20 {ECO:0008006|Google:ProtNLM};
GN Name=LOC101111693 {ECO:0000313|Ensembl:ENSOARP00000009847.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000009847.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000009847.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000009847.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000009847.1}
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; AMGL01051290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PHD0; -.
DR SMR; W5PHD0; -.
DR STRING; 9940.ENSOARP00000009847; -.
DR PaxDb; 9940-ENSOARP00000009847; -.
DR Ensembl; ENSOART00000009989.1; ENSOARP00000009847.1; ENSOARG00000009177.1.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_012714_4_0_1; -.
DR OMA; CGASECI; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000009177; Expressed in testis and 2 other cell types or tissues.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905:SF239; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 26B-RELATED; 1.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 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; 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:UP000002356};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..752
FT /note="ADAM metallopeptidase domain 20"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004870938"
FT TRANSMEM 676..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..385
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 391..477
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 615..648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 647..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 344..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 449..469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 638..647
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 752 AA; 84375 MW; EC72C3E0B2612978 CRC64;
LWLKVFLFLP EWPQVGHSQR VGPPEVVIPL RVTPTGRGMK LQGWLCYKLH FGGQRHVVHM
KVKKNFLSKN FPVFTYADTG VLLEDQPFVQ DDCYYRGYVE GDPESLVSLN NCFGGFQGML
QTNDIVYEIE PKRFSTAFEH LIYKLDNEET NFSYFRCGLT DEEIAGQLKF QESINSTLKQ
SSYAGWWTHS YFLEVAVVVD HSRYLHHGSN ASLVQKEVFL VLNVVSDVLK TLDLELLLMG
IEIWTERSLV ALGGGIRKAL DEFCKWKENG LQNRVPHDLA HIFVKRHYGN TIGWSFIGTV
CSDRYSCGIE SFHNEGVSTL SHVVIHETSH VLGMNHDNTN LCKCAASRCI MFPYVGVTTK
YTNCSYADYW NLVHRRHCLY IAPDPLTVLR ETRCGNSVVE EGEECDCGPV KKCTADPCCQ
LNCTMTAGVN CSSGLCCHNC RFMPSGTVCR KVENECDLPE WCNGTSSQCP EDVYMQDGTS
CTGGGYCYEK RCNERNEQCR QIFGQEARSA NVSCYRAVNT RGDRFGNCGI TASSYEKCNM
SDSLCGRIQC ENVKGLPLMR GHTTLHWTKI NNNTCWGVDY HHGIRTADIG DVKDGTMCGP
QNICISRKCV SSSTLPRFCS PQFCSLRGIC NNRHHCHCDP KWDPPTCQQK GRGGSVDSGP
PPASQAEERV EKSNPLPYLL IPLLLLLLCL LLLLLLFMRR KKTDDKAEKP VPTDDKAEKP
VPTDAKAEMP VPTDAKAETP VPTDAKAETP VP
//
