GenomeNet

Database: UniProt
Entry: Q8TC27
LinkDB: Q8TC27
Original site: Q8TC27 
ID   ADA32_HUMAN             Reviewed;         787 AA.
AC   Q8TC27; Q8TC42;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 32;
DE            Short=ADAM 32;
DE   Flags: Precursor;
GN   Name=ADAM32; ORFNames=UNQ5982/PRO21340;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-467.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [2]
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., Gloeckner 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.J., 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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-98; GLY-160
RP   AND SER-467.
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 17-31.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12568724; DOI=10.1016/S0378-1119(02)01202-7;
RA   Choi I., Woo J.-M., Hong S., Jung Y.-K., Kim D.H., Cho C.;
RT   "Identification and characterization of ADAM32 with testis-predominant
RT   gene expression.";
RL   Gene 304:151-162(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
CC   -!- FUNCTION: May play a role in sperm development and fertilization
CC       This is a non-catalytic metalloprotease-like protein.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC       {ECO:0000269|PubMed:12568724}.
DR   EMBL; AY358739; AAQ89099.1; -; mRNA.
DR   EMBL; AC105091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026085; AAH26085.1; -; mRNA.
DR   EMBL; BC026169; AAH26169.1; -; mRNA.
DR   EMBL; BC028702; AAH28702.1; -; mRNA.
DR   EMBL; BC030014; AAH30014.1; -; mRNA.
DR   EMBL; BC030698; AAH30698.1; -; mRNA.
DR   EMBL; BC034975; AAH34975.1; -; mRNA.
DR   CCDS; CCDS47846.1; -.
DR   RefSeq; NP_001300923.1; NM_001313994.1.
DR   RefSeq; NP_659441.3; NM_145004.6.
DR   UniGene; Hs.521545; -.
DR   ProteinModelPortal; Q8TC27; -.
DR   SMR; Q8TC27; -.
DR   BioGrid; 128451; 26.
DR   IntAct; Q8TC27; 1.
DR   STRING; 9606.ENSP00000369238; -.
DR   MEROPS; M12.953; -.
DR   iPTMnet; Q8TC27; -.
DR   PhosphoSitePlus; Q8TC27; -.
DR   BioMuta; ADAM32; -.
DR   DMDM; 296434389; -.
DR   EPD; Q8TC27; -.
DR   PaxDb; Q8TC27; -.
DR   PeptideAtlas; Q8TC27; -.
DR   PRIDE; Q8TC27; -.
DR   ProteomicsDB; 74084; -.
DR   DNASU; 203102; -.
DR   Ensembl; ENST00000379907; ENSP00000369238; ENSG00000197140.
DR   Ensembl; ENST00000615420; ENSP00000484817; ENSG00000275594.
DR   GeneID; 203102; -.
DR   KEGG; hsa:203102; -.
DR   UCSC; uc003xmt.5; human.
DR   CTD; 203102; -.
DR   DisGeNET; 203102; -.
DR   EuPathDB; HostDB:ENSG00000197140.14; -.
DR   GeneCards; ADAM32; -.
DR   HGNC; HGNC:15479; ADAM32.
DR   HPA; HPA044156; -.
DR   HPA; HPA062151; -.
DR   neXtProt; NX_Q8TC27; -.
DR   OpenTargets; ENSG00000197140; -.
DR   PharmGKB; PA134932610; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000161015; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q8TC27; -.
DR   KO; K16070; -.
DR   OMA; SVIVTQM; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q8TC27; -.
DR   TreeFam; TF314733; -.
DR   ChiTaRS; ADAM32; human.
DR   GenomeRNAi; 203102; -.
DR   PRO; PR:Q8TC27; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000197140; Expressed in 106 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q8TC27; baseline and differential.
DR   Genevisible; Q8TC27; HS.
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; 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; 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; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000269|PubMed:15340161}.
FT   PROPEP       17    174       {ECO:0000255}.
FT                                /FTId=PRO_0000029138.
FT   CHAIN       175    787       Disintegrin and metalloproteinase domain-
FT                                containing protein 32.
FT                                /FTId=PRO_0000029139.
FT   TOPO_DOM    175    682       Extracellular. {ECO:0000255}.
FT   TRANSMEM    683    703       Helical. {ECO:0000255}.
FT   TOPO_DOM    704    787       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      186    383       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      391    479       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      622    654       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    480    502       Cys-rich.
FT   MOD_RES      17     17       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:20068231}.
FT   CARBOHYD     39     39       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    125    125       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    465    465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    598    598       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    295    378       {ECO:0000250}.
FT   DISULFID    337    362       {ECO:0000250}.
FT   DISULFID    339    344       {ECO:0000250}.
FT   DISULFID    450    471       {ECO:0000250}.
FT   DISULFID    626    636       {ECO:0000250}.
FT   DISULFID    630    642       {ECO:0000250}.
FT   DISULFID    644    653       {ECO:0000250}.
FT   VARIANT      98     98       Q -> R (in dbSNP:rs17856744).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_055241.
FT   VARIANT     160    160       S -> G (in dbSNP:rs17852343).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_055242.
FT   VARIANT     327    327       L -> V (in dbSNP:rs9643859).
FT                                /FTId=VAR_055243.
FT   VARIANT     467    467       T -> S (in dbSNP:rs7845771).
FT                                {ECO:0000269|PubMed:12975309,
FT                                ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_051591.
FT   VARIANT     658    658       K -> N (in dbSNP:rs13277386).
FT                                /FTId=VAR_055244.
FT   VARIANT     778    778       D -> E (in dbSNP:rs28705715).
FT                                /FTId=VAR_061739.
SQ   SEQUENCE   787 AA;  87948 MW;  841EDA9EFF483A2C 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
     AGVALYPKEI TLEAFAVIVT QMLALSLGIS YDDPKKCQCS ESTCIMNPEV VQSNGVKTFS
     SCSLRSFQNF ISNVGVKCLQ NKPQMQKKSP KPVCGNGRLE GNEICDCGTE AQCGPASCCD
     FRTCVLKDGA KCYKGLCCKD CQILQSGVEC RPKAHPECDI AENCNGTSPE CGPDITLING
     LSCKNNKFIC YDGDCHDLDA RCESVFGKGS RNAPFACYEE IQSQSDRFGN CGRDRNNKYV
     FCGWRNLICG RLVCTYPTRK PFHQENGDVI YAFVRDSVCI TVDYKLPRTV PDPLAVKNGS
     QCDIGRVCVN RECVESRIIK ASAHVCSQQC SGHGVCDSRN KCHCSPGYKP PNCQIRSKGF
     SIFPEEDMGS IMERASGKTE NTWLLGFLIA LPILIVTTAI VLARKQLKKW FAKEEEFPSS
     ESKSEGSTQT YASQSSSEGS TQTYASQTRS ESSSQADTSK SKSEDSAEAY TSRSKSQDST
     QTQSSSN
//
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