ID A0A2K6UWQ7_SAIBB Unreviewed; 714 AA.
AC A0A2K6UWQ7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=ADAM metallopeptidase domain 21 {ECO:0008006|Google:ProtNLM};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000036331.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000036331.1}
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 AlphaFoldDB; A0A2K6UWQ7; -.
DR Ensembl; ENSSBOT00000053263.1; ENSSBOP00000036331.1; ENSSBOG00000034308.1.
DR GeneTree; ENSGT00940000162712; -.
DR OMA; WWTHSWF; -.
DR Proteomes; UP000233220; 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; 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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF116; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 21; 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.
DR PROSITE; PS01186; EGF_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:UP000233220};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..714
FT /note="ADAM metallopeptidase domain 21"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014369313"
FT TRANSMEM 674..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..390
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 398..484
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 350..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 456..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 714 AA; 79795 MW; 5216B760BCB3458E CRC64;
MLVDGTLQHI RVTLLLLLLG VCFSISGYFQ AGPSQHLTPS EVVIPLKVIS RGRGAKAPGW
LSYSLRFGGQ RHVVHMRVKK LLVSRHLPVF TYTEQRALLE DRPFIPDDCY YHGFVEGAPE
SLVVFSACFG GLRGVLQING LTYEIEPIRH SATFEHLIYK INSNETQFPA MRCGLTEKEV
ARQRLESEEA ENSALKPNSV GDWWTHAWFL ELVVVLNHDF FIYSQSNISK VQEDVFLVVN
IVDSMFKQLG TYILLIGIKI WNQGNVFPMT GITQVLNDFS QWKHISLSQL QHDAAHIILG
LAYIAGICLL PIDCGVDNFQ GDTWSLFANT VAHELGHTLG MWHDEEFCFC GERGCIMSTF
RVPAEKFTNC SYADFMKTTL NQGSCLHDPP RLGEIFMLKR CGNGVVEREE QCDCGSVQQC
EQDACCLSNC TLRPGAACAF GLCCKDCKFM PSGELCRQKV NECDLPEWCN GSSHQCPEDR
YVQDGVPCSD SAYCYQKSCN NHDQHCREIF GKDAKSASGN CYKEINSQGN RFGHCGINGT
TYLKCHISDV FCGRVQCENV RDIPLLQDHF TLQHAHINGV TCWSIDYHLR MNTPDIGEVK
DGTVCGPGKI CIHKKCVSLS VLSHVCLPET CNMKGICNNK HHCHCGHGWS PPYCLHRGYG
GSVDSGPASA KRRVFLTVIM IPSLSVLIFL FTIGLLMYLR QRSGPKETKA HSSG
//
