ID D2H047_AILME Unreviewed; 974 AA.
AC D2H047;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE Flags: Fragment;
GN ORFNames=PANDA_002765 {ECO:0000313|EMBL:EFB26344.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB26344.1};
RN [1] {ECO:0000313|EMBL:EFB26344.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL192401; EFB26344.1; -; Genomic_DNA.
DR RefSeq; XP_019650293.1; XM_019794734.1.
DR MEROPS; M12.016; -.
DR GeneID; 100477539; -.
DR KEGG; aml:100477539; -.
DR CTD; 649; -.
DR InParanoid; D2H047; -.
DR OrthoDB; 2873870at2759; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF34; CUB AND SUSHI DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 110..309
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 311..423
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 424..536
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 536..577
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 580..692
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 735..847
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 848..964
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 203
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 172..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 174..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFB26344.1"
FT NON_TER 974
FT /evidence="ECO:0000313|EMBL:EFB26344.1"
SQ SEQUENCE 974 AA; 110340 MW; B5140A0D815265B4 CRC64;
LLLWLLLLPR PGRPLDLADY TYDLGEEDDS EPVNYXXXXA AAFLGDIALD EEDLRAFQEQ
QAVDLRQRAT HRASIKTAGN SSTFDCQSTN GQLQRRSCGR WRGRSRSRRA ATSRPERVWP
DGVIPFVIGG NFTGSQRAVF RQAMRHWEKH TCVTFLERTD EDSYIVFTYR PCGCCSYVGR
RGGGPQAISI GKNCDKFGIV VHELGHVIGF WHEHTRPDRD RHVSIIRENI QPGQEYNFLK
MELQEVESLG ETYDFDSIMH YARNTFSRGI FLDTIVPKYE VNGVKPPIGQ RTRLSKGDIA
QARKLYKCPA CGETLQDSTG NFSSPEYPNG YSAHMHCVWR ISVTPGEKII LNFTSMDLYR
SRLCWYDYVE VRDGFWRKAP LRGRFCGGKL PEPIVSTDSR LWVEFRSSSN WVGKGFFAVY
EAICGGDVKK DNGHIQSPNY PDDYRPSKVC VWRIQVSEGF HVGLTFQSFE IERHDSCAYD
YLEVRDGHSE SSALIGRYCG YEKPDDIKST SSRLWLKFVS DGSINKAGFA VNFFKEVDEC
SRPNRGGCEQ RCLNTLGSYK CSCDPGYELA PDKRRCEAAC GGFLTKLNGS ITSPGWPKEY
PPNKNCIWQL VAPTQYRISL QFDFFETEGN DVCKYDFVEV RSGLTADSKL HGKFCGSEKP
EVITSQYNNM RVEFKSDNTV SKKGFKAHFF SDKDECSKDK ACQQDCVNTF GSYECQCRSG
FVLHDNKHDC KEAGCDHKVT STSGTITSPN WPDKYPSKKE CTWAISSTPG HRVKLTFVEM
DIESQPECAY DHLEVYDGRD AKAPALGRFC GSKKPEPVLA TGSRMFLRFY SDNSVQRKGF
QASHSTECGG QVRAEVKTKD LYSHAQFGDN NYPGGVDCEW VIVAEEGYGV ELVFQTFEVE
EETDCGYDYM ELFDGYDSTA PRLGRYCGSG PPEEVYSAGD SVLVKFHSDD TITKKGFHLR
YTSTKFQDTL HSRK
//
