ID H2R9U7_PANTR Unreviewed; 629 AA.
AC H2R9U7; A0A2J8N7J8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=ADAM metallopeptidase domain 32 {ECO:0000313|Ensembl:ENSPTRP00000053184.4};
GN Name=ADAM32 {ECO:0000313|Ensembl:ENSPTRP00000053184.4,
GN ECO:0000313|VGNC:VGNC:11932};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000053184.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000053184.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000053184.4}
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:PRU00076}.
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DR EMBL; AACZ04065567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04065568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2R9U7; -.
DR Ensembl; ENSPTRT00000059918.4; ENSPTRP00000053184.4; ENSPTRG00000031006.4.
DR VGNC; VGNC:11932; ADAM32.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161015; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000031006; Expressed in testis and 18 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..629
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015093424"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..306
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 302..373
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 516..548
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 607..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 520..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 538..547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 629 AA; 70916 MW; F41CF2C1535F4F52 CRC64;
MFRLWLLLAG LCGLLASRPG FQNSLLQIVI PEKIQTNTND SSEIEYEQIS YIIPIDEKLY
TVHLKQRYFL ADNFMIYLYN QGSMNTYSSD IQTQCYYQGN IEGYPDSMVT LSTCSGLRGI
LQFENVSYGI EPLESAVEFQ HVLYKLKNED NDIAIFIDRS LKEQPMDDNI FISEKSEPAV
PDLFPLYLEM HIVVDKTLFD YWGSDSMIVT NKVIEIVGLA NSMFTQFKVT IVLSSLELWS
DENKISTVGE ADELLQKFLE WKQSYLNLRP HDIAYLLIYT DYPRYLGAVF PGTMCITRYS
AGVALQCGPA SCCDFRTCVL KDGAKCYKGL CCKDCQILQS GVECRPKAHP ECDIAENCNG
SSPECGPDIT LINGLSCKNN KFICYDGDCH DLDARCESVF GKGSRNAPFA CYEEIQSQSD
RFGNCGRDRN NKYVFCGWRN LICGRLVCTY PTRKPFHQEN GDVIYAFVRD SVCITVDYKL
PRTVPDPLAV KNGSQCDIGR VCVNRECVES RIIKASAHVC SQQCSGHGVC DSRNKCHCSP
GYKPPNCQIR SKGFSIFPEE DMGSIMERAS GKTENTWLLG FLIALPILIV TTAIVLARKQ
LKKWFAKEEE FPSSESKSQE STQTQSSSN
//
