ID L8Y547_TUPCH Unreviewed; 1184 AA.
AC L8Y547;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|EMBL:ELV10090.1};
GN ORFNames=TREES_T100006006 {ECO:0000313|EMBL:ELV10090.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV10090.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; KB368801; ELV10090.1; -; Genomic_DNA.
DR AlphaFoldDB; L8Y547; -.
DR STRING; 246437.L8Y547; -.
DR MEROPS; M12.976; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; L8Y547; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 6.10.250.3410; DBF zinc finger; 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 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 InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF114; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 11; 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 Pfam; PF07535; zf-DBF; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SMART; SM00586; ZnF_DBF; 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; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51265; ZF_DBF4; 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 Integrin {ECO:0000313|EMBL:ELV10090.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
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|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00600}.
FT TRANSMEM 1110..1133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..125
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT DOMAIN 614..813
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 819..906
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 1048..1085
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 878..898
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 1075..1084
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1184 AA; 127690 MW; 464BA9B251B9FA51 CRC64;
MSRGKELLQK AIRNQGSSSG GSSGSSSLLT SARSWGVRIL HVDVAKLKAP FLKIEDESRK
PRDREPSLRS VTRAVSRRKK GYCECCQEAF DELRVHLESA QHQSFAREAR SYAEVDRIIA
QLNHSFADIP SHASSSRWAG SLASDRDLLS PETSPPSQPS LALGAPEQDG TEDSMKTPTE
PEPAGTGEVP GPAVSCQDML VDPQETPAPR SPARQSPLTS SPHVDLCSGL DLALVGHKRK
VLFPSGNAEK RPGATSPQAS FFVPRATSPC STRTPSDKHL SLPLPDHNSR PLTSPLPLCH
TQTCLSFPDA LPWQPTDRPA KFWATQPRWP GGGWPLRSED SECVAPGPVS QQADQLPSCS
MAPGQLSAHL QAANLQPPTE PAESQCTSLP PLLASGGASC SRWLWAPQLL QMPCLPASQL
PPPPPPSAGR ELLLSGLVFL GLGAQGPAGA LHWGGSPQVG GPEAPEITQP SRLVGESSGG
EVRKQQLDTR VRQERPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS QYVERHFSPE
GTTQHSTGAG DHCYYQGKLR GNPRSFAAIS TCQGLHGVFS DGNLTYIVEP QEMAGPWGAP
QVRRGHPTVH SETKYVELIV INDHQLFEQM RQSVVLTSNF AKSVVNLADV IYKEQLNTRI
VLVAMETWAD GDKIQVQDDL LETLARLMVY RREGLPEPSD ATHLFSGRTF QSASSGAAYV
GGICSLSRGG GVNEYGNMGA MAVTLAQTLG QNLGMMWNKH RSSAGDCKCP DLWLGCIMED
TGFYLPRKFS RCSIDEYNQF LQEGGGSCLF NKPLKLLDPP ECGNGFVEAG EECDCGSVQE
CSRSGGNCCK KCTLTHDAMC SDGLCCRRCK YEPRGVSCRE AVNECDIAET CTGDSSQCPP
NLHKLDGYYC DHEQGRCYGG RCKTRDRQCQ ALWGHAAADR FCYEKLNVEG TERGNCGRKG
SGWVQCNKQD VLCGFLLCVN ISGAPRLGDL GADISSVTFY HQGKELDCRG GHVQLADGSD
LSYVEDGTAC GPNMLCLDHR CLPASAFNFS TCPGSGERRV CSHHGVCSNE GKCICQPDWT
GKDCSIHNPL PTAPPTGETE RYKGPSGTNI IIGSIAGAVL VAAIVLGGTG WGFKPALGTK
CHLLHGMLTE HPSYRGLHRP EQTPDCPVLI RKAIHKVHLA PDGR
//
