ID A0A2R9CDH2_PANPA Unreviewed; 516 AA.
AC A0A2R9CDH2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ADAM metallopeptidase domain 7 {ECO:0000313|Ensembl:ENSPPAP00000039985.1};
GN Name=ADAM7 {ECO:0000313|Ensembl:ENSPPAP00000039985.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000039985.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000039985.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000039985.1}
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:PRU00276}.
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DR EMBL; AJFE02083077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02083078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02083079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02083080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9CDH2; -.
DR Ensembl; ENSPPAT00000062898.1; ENSPPAP00000039985.1; ENSPPAG00000042630.1.
DR GeneTree; ENSGT00940000161406; -.
DR Proteomes; UP000240080; Chromosome 8.
DR Bgee; ENSPPAG00000042630; Expressed in adult mammalian kidney and 1 other cell type or tissue.
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; 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:SF21; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 7; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
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 441..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..166
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 174..260
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 124..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 232..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 516 AA; 58126 MW; 951CBD5842535ED0 CRC64;
MVNFVNMIYK TLNIHVTLVG IEIWTHEDKI ELYSNIETTL LHFSFWQEKI LKTRKDFDHV
VLLSGKWLYS HVQGISYPGG MCLPYYSTSI IKDLLPDTNI IANRMAHQLG HNLGMQHDEF
PCTCPSGKCV MDSDGSIPAL KFSKCSQNQY HQYLKDYKPT CMLNIPFPYN FDDFQFCGNK
KLDEGEECDC GPAQECTNPC CDAHTCVLKP GFTCAEGECC ESCQIKKAGS ICRPAKDECD
FPEMCTGHSP ACPKDQFRVN GFPCKNSEGY CFMGKCPTRE DQCSELFDDE AIESHDICYK
MNTKGNKFGY CKNKENRFLP CKEKDVRCGK VYCTGGELSS LLGEDKTYHL KDPQQNATVK
CKTIFLYHDS TDIGLVASGT KCGEGMVCNN GECLNMEKVY ISTNCPSQCR ENPVDGHGLQ
CHCEEGQAPV ACEETLNVTN ITVLVVVLVL VIVGIGVLIL LVRYRKCIKL KQVQSPPTET
LGVENKGYFG DEQQIRTEPI LPEIHFRNHL LYGRHQ
//
