ID A0A2K5M2Q0_CERAT Unreviewed; 790 AA.
AC A0A2K5M2Q0;
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 32 {ECO:0000313|Ensembl:ENSCATP00000019473.1};
GN Name=ADAM32 {ECO:0000313|Ensembl:ENSCATP00000019473.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000019473.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000019473.1}
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:PRU00076}.
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DR AlphaFoldDB; A0A2K5M2Q0; -.
DR STRING; 9531.ENSCATP00000019473; -.
DR Ensembl; ENSCATT00000043655.1; ENSCATP00000019473.1; ENSCATG00000033525.1.
DR GeneTree; ENSGT00940000161015; -.
DR OMA; GWQCLCP; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000033525; Expressed in cerebellum and 5 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF24; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 32; 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 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.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..790
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014381467"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 188..385
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 393..481
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 624..657
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 721..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 341..346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 647..656
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 790 AA; 88473 MW; 302867A777899166 CRC64;
MFRLWLLLAR LCGLLASRRG FQNSLLQIVI PEKIQTNTSD SSEIEYEQIS YIIPIDEKPY
TVHLKQRYFL ADNFMIYLYD QGSMNARSSD IQTQCYYQGN IEGYPDSMVT LSTCSGLRGI
LQFENVSYAI EPLESAVEFQ HVLYKLENED NDIAIFSENN RSLEEHPMDD NISISEQSEP
AVPVLFPLYL EMHIVVDKAL YDYWGSDSMI VTNKVIEIVG LANSMFAQFK VTIVLSSLEV
WSDENKISTV GEADELLKRF LEWKQSYLNL RPHDIAYLLI YRDYPDYVGA TFPGKMCITR
YSAGVALYPK EITLEAFSVI VTQMLALSLG ISYDDPKKCR CSESICIMNP EALQSNGVKT
FSSCSLRSFQ NFISNVGAKC LQNKPQMQKK SPKPVCGNGR LEGSEICDCG TEAQCGPASC
CDFRTCVLKD GAQCYRGSCC RDCQILQSGV ECRPKAHPEC DIAENCNGSS PECGPDITLF
NGLPCKNSKF ICYDGDCHDL DARCESVFGK GSRNAPFACY EEIQSQADRF GNCGRDRNNK
YVFCGWRNLI CGRLVCTYPT RKPFHQENGD VIYAFVRDSV CVTIDYKLPR TVPDPLTVKN
GSQCDVGRIC VNRECVESRK IKATALVCSE HICSGHGVCD SRQKCICSPG YNPPSCRTRS
KGFPIFPKED MDSIMERASG KTENTWLLGF SVVLPILIVT TIVVLARKHL KKWFIKEEEF
PSSESKSEGS TQTYASQSIS EGSTQTYASR TRSESSGQAD TSKSKSEDST QAYTSRSKSQ
ESTQTQSSSN
//
