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Database: UniProt
Entry: A0A2K5VEY7_MACFA
LinkDB: A0A2K5VEY7_MACFA
Original site: A0A2K5VEY7_MACFA 
ID   A0A2K5VEY7_MACFA        Unreviewed;       750 AA.
AC   A0A2K5VEY7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=ADAM metallopeptidase domain 32 {ECO:0000313|Ensembl:ENSMFAP00000023268.2};
GN   Name=ADAM32 {ECO:0000313|Ensembl:ENSMFAP00000023268.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000023268.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000023268.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000023268.2}
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; A0A2K5VEY7; -.
DR   Ensembl; ENSMFAT00000031401.2; ENSMFAP00000023268.2; ENSMFAG00000043270.2.
DR   VEuPathDB; HostDB:ENSMFAG00000043270; -.
DR   GeneTree; ENSGT00940000161015; -.
DR   Proteomes; UP000233100; Chromosome 8.
DR   Bgee; ENSMFAG00000043270; Expressed in lung and 6 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:UP000233100};
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..750
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030051489"
FT   TRANSMEM        690..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          192..389
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          397..485
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          628..661
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        345..350
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        651..660
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   750 AA;  84375 MW;  20CF8BF6967C92CD CRC64;
     TIFLFFILSY LQGILSWKPN NFSFQNSLLQ IVIPEKIQTN TSDGSEIEYE QISYIIPIDE
     KPYTVHLKQR YFLADNFMIY LYDQGSMNAR SSDIQTQCYY QGNIEGYPDS MVTLSTCSGL
     RLGILQFENV SYAIEPLESA VEFQHVLYKL DNEDNDIAIF SENNRSLEEH PMDDNISISE
     QSEPAVPDLF PLYLEMHIVV DKALYDYWGS DSMVVTNKVI EIVGLANSMF AQFKVTIVLS
     SLEVWSDENK ISTVGEADEL LKRFLEWKQS YLNLRPHDIA YLLIYRDYPD YVGATFPGKM
     CITRYSAGVA LYPKEITLEA FSVIVTQMLA LSLGISYDDP KKCRCSESIC IMNPEALQSN
     GVKTFSSCSL RSFQNFISNV GAKCLQNKPQ MQGKSPKPVC GNGRLEGSEM CDCGTEAQCG
     PASCCDFRTC VLKDGAQCYR GSCCRDCQIL QSGVECRPKA HPECDIAENC NGSSPECGPD
     ITLFNGLPCK NSKFICYDGD CHDLDARCES VFGKGSRNAP FACYEEIQSQ ADRFGNCGRD
     RNNKYVFCGW RNLICGRLVC TYPTRKPFHQ ENGDVIYAFV RDSVCVTVDY KLPRTVPDPL
     TVKNGSQCDV GRICVNRQCV ESRKIKATAL VCSEYTCSGH GVCDSRQKCV CSPGYNPPSC
     QTRSKGFPIF PKEDMDSIME RASGKTENTW LLGFSVVLPI LIVTTIVVLA RKHLKKWFIK
     EEEFPSIIEL SVERGRTRIY NICSFLIEGG
//
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