ID   A0A0G2JPC8_HUMAN        Unreviewed;       629 AA.
AC   A0A0G2JPC8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   12-SEP-2018, entry version 29.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 32 {ECO:0000313|Ensembl:ENSP00000483377};
GN   Name=ADAM32 {ECO:0000313|Ensembl:ENSP00000483377};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000483377, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000213|PubMed:17081983}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000483377, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Glockner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA   O'Leary S.B., O'Neill K., Parker S.C., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [3] {ECO:0000213|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:ra3-RA3(2010).
RN   [4] {ECO:0000313|Ensembl:ENSP00000483377}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00068}.
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DR   EMBL; AC105091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC245594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; A0A0G2JPC8; -.
DR   PeptideAtlas; A0A0G2JPC8; -.
DR   Ensembl; ENST00000618895; ENSP00000483377; ENSG00000275594.
DR   HGNC; HGNC:15479; ADAM32.
DR   ChiTaRS; ADAM32; human.
DR   Proteomes; UP000005640; Chromosome 8.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008979; Galactose-bd-like_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   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; SSF57552; 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   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00517240};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:A0A0G2JPC8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    629       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002546657.
FT   TRANSMEM    577    597       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      186    306       Peptidase M12B.
FT                                {ECO:0000259|PROSITE:PS50215}.
FT   DOMAIN      302    373       Disintegrin.
FT                                {ECO:0000259|PROSITE:PS50214}.
FT   DOMAIN      516    548       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DISULFID    520    530       {ECO:0000256|PROSITE-ProRule:PRU00076}.
FT   DISULFID    538    547       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   629 AA;  70948 MW;  91A4513AE9DF031F CRC64;
     MFRLWLLLAG LCGLLASRPG FQNSLLQIVI PEKIQTNTND SSEIEYEQIS YIIPIDEKLY
     TVHLKQRYFL ADNFMIYLYN QGSMNTYSSD IQTQCYYQGN IEGYPDSMVT LSTCSGLRGI
     LQFENVSYGI EPLESAVEFQ HVLYKLKNED NDIAIFIDRS LKEQPMDDNI FISEKSEPAV
     PDLFPLYLEM HIVVDKTLYD YWGSDSMIVT NKVIEIVGLA NSMFTQFKVT IVLSSLELWS
     DENKISTVGE ADELLQKFLE WKQSYLNLRP HDIAYLLIYM 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 FPSSESKSQD STQTQSSSN
//