ID A0A2K6K1D1_RHIBE Unreviewed; 754 AA.
AC A0A2K6K1D1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ADAM metallopeptidase domain 7 {ECO:0000313|Ensembl:ENSRBIP00000005093.1};
GN Name=ADAM7 {ECO:0000313|Ensembl:ENSRBIP00000005093.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000005093.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000005093.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000005093.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017739971.1; XM_017884482.1.
DR AlphaFoldDB; A0A2K6K1D1; -.
DR Ensembl; ENSRBIT00000025340.1; ENSRBIP00000005093.1; ENSRBIG00000022906.1.
DR GeneID; 108537256; -.
DR CTD; 8756; -.
DR GeneTree; ENSGT00940000161406; -.
DR OMA; RFSTWQE; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..754
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014326238"
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 754 AA; 85849 MW; 97FB5F6D267F1249 CRC64;
MLPGCIFLMI LLILQVKEKI ILGVEGQQLV HPKKLPLIQK RDIGHTHHDD IEETYEEELL
YEIKLNRKTL VLHLLRSREF LGSNYSETFY SMKGEAFTRH LQIMDHCFYQ GSIVHEYDSA
ASISTCNGLR GFFRVNDQRY LIEPVKYSDE GEHLVFKYNP RVPYVANYSC TELNLTRKTV
PGDTESEGDP KMKAIHNEKY IELFVVADDT VYRRNSHPHN KLRNRIWGMV NFVNMIYKTL
NIHVTLVGIE IWTHEDKIEL HSNIETTLLR FSSWQERILK TRKDFDHVVL LSGKWIYTHV
QGISYPAGMC LPYYSTSIIK DLLPDANIIA NRMAHQLGHN LGMQHDEFPC TCPSGKCVMD
SDGSIPALKF SKCSQNQYHT YLKDYKPTCM LNIPFPCNFD DFQFCGNKKL DEGEECDCGP
PQECTNPCCD AHTCVLKPGF TCAEGECCES CQIKKAGSIC RPAEDECDFP EMCTGHSPAC
PKDQFRVNGF PCKNSEGYCF MGKCPTRGDQ CSELFDDEAI ESHDICYKMN TKGNKFGYCK
NKENKFLPCE EKDVRCGKIY CTGGELSYLL GEDKTYHLKD PQQNATVICK TIFLYRDSTD
IGLVASGTKC RDGMVCNNGE CLNMEKVYNS TNCPSQCHEN PMDDHGLHCQ CEEGQAPVAW
EETLNVTNVV ILVVVLVLVI VGIGVLILLI RYQKCIKLKQ VQSPPIETLG VENKGYFGDE
QQMRTEPILP EIRFLNKPAR EDSRGIADPN QSAK
//
