ID H2PPU9_PONAB Unreviewed; 775 AA.
AC H2PPU9; A0A2J8X4W2; A0A6D2W3M8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=ADAM metallopeptidase domain 7 {ECO:0000313|Ensembl:ENSPPYP00000020672.1};
DE SubName: Full=ADAM7 isoform 3 {ECO:0000313|EMBL:PNJ77070.1};
GN Name=ADAM7 {ECO:0000313|Ensembl:ENSPPYP00000020672.1};
GN ORFNames=CR201_G0005179 {ECO:0000313|EMBL:PNJ77070.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000020672.1, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000020672.1, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ77070.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ77070.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000020672.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:PRU00276}.
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DR EMBL; NDHI03003372; PNJ77070.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000020672; -.
DR Ensembl; ENSPPYT00000021501.2; ENSPPYP00000020672.1; ENSPPYG00000018447.3.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161406; -.
DR HOGENOM; CLU_012714_6_0_1; -.
DR OMA; RFSTWQE; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:1905867; P:epididymis development; IEA:Ensembl.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IEA:Ensembl.
DR GO; GO:1902492; P:positive regulation of sperm capacitation; IEA:Ensembl.
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; IPR002870; Peptidase_M12B_N.
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; 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.
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:UP000001595};
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..775
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014575205"
FT TRANSMEM 669..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 352..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 460..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 775 AA; 88205 MW; EFCB2C1AF5A619A7 CRC64;
MLPGCIFLMI LLIPQVKEKF ILGVEGQQLV HPKKLPLIQK RDTGHTHDDD IPKMYEEELL
YEIKLNRKTL VLHLLRSREF LGSNYSETFY SMKGEAFTRH PQIMDHCFYQ GSIVHEYDSA
ASISTCNGLR GFFRINDQRY LIEPVKYSDE GEHLVFKYNL RVPYVANYSC TELNFTRKTV
PGDNESEEDS KMKEIHDEKY IELFIVADDT VYRRNGHPHN KLRNRIWGMV NFVNMIYKTL
NIHVTLVGIE IWTHEDKIEL YSNIETTLLR FSFWQEKILK TRKDFDHVVL LSGKWLYSHV
QGISYPGGMC LPYYSTSIIK DLLPDTNIIA NRMAHQLGHN LGMQHDEFPC TCPSGKCVMD
SDGSIPALKF SKCSQNQYHQ YLKDYKPTCM LNIPFPYNFD DFQFCGNKKL DEGEECDCGP
AQECTNPCCD AHTCVLKPGF TCAEGECCES CQIKKAGSIC RPAKDECDFP EMCTGHSPAC
PKDQFRVNGF PCKNSEGYCF MGKCPTREDQ CSELFDDEAI ESHDICYKMN TKGNKFGYCK
NEENGFLPCE EKDVRCGKIY CTGGELSSLL GEDKTYHLKD PQQNATVECK TIFLYRDSTD
IGLVASGTKC GDGMVCNNGE CLNMEKVYIS TNCSSQCHEN PVDGHGLQCH CEEGQVPVAC
EETLNVTNIT ILVVVLVVVI VGIGVLILLV RYRKCIKLKQ VQRPIETLGV ENKGYFGDEQ
QIRTEPILPE IHFLNQRTPE SLESLPTSFS SPHYITMKPA SKDSRGITDP NQSAK
//
