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   27-MAR-2024, entry version 170.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   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., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., 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., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., 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 AND
RP   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 project:
RT   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 verified
RT   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 gene
RT   expression.";
RL   Gene 304:151-162(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP   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., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP   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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
CC   -!- FUNCTION: May play a role in sperm development and fertilization This
CC       is a non-catalytic metalloprotease-like protein. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8TC27; P56748: CLDN8; NbExp=3; IntAct=EBI-18273040, EBI-10215641;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:12568724}.
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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   AlphaFoldDB; Q8TC27; -.
DR   SMR; Q8TC27; -.
DR   BioGRID; 128451; 28.
DR   IntAct; Q8TC27; 22.
DR   STRING; 9606.ENSP00000369238; -.
DR   MEROPS; M12.960; -.
DR   GlyCosmos; Q8TC27; 4 sites, No reported glycans.
DR   GlyGen; Q8TC27; 4 sites.
DR   iPTMnet; Q8TC27; -.
DR   PhosphoSitePlus; Q8TC27; -.
DR   BioMuta; ADAM32; -.
DR   DMDM; 296434389; -.
DR   EPD; Q8TC27; -.
DR   MassIVE; Q8TC27; -.
DR   PaxDb; 9606-ENSP00000369238; -.
DR   PeptideAtlas; Q8TC27; -.
DR   ProteomicsDB; 74084; -.
DR   Antibodypedia; 23785; 183 antibodies from 25 providers.
DR   DNASU; 203102; -.
DR   Ensembl; ENST00000379907.9; ENSP00000369238.4; ENSG00000197140.15.
DR   Ensembl; ENST00000615420.4; ENSP00000484817.1; ENSG00000275594.4.
DR   GeneID; 203102; -.
DR   KEGG; hsa:203102; -.
DR   MANE-Select; ENST00000379907.9; ENSP00000369238.4; NM_145004.7; NP_659441.4.
DR   UCSC; uc003xmt.5; human.
DR   AGR; HGNC:15479; -.
DR   CTD; 203102; -.
DR   DisGeNET; 203102; -.
DR   GeneCards; ADAM32; -.
DR   HGNC; HGNC:15479; ADAM32.
DR   HPA; ENSG00000197140; Tissue enriched (testis).
DR   MIM; 618602; gene.
DR   neXtProt; NX_Q8TC27; -.
DR   OpenTargets; ENSG00000197140; -.
DR   PharmGKB; PA134932610; -.
DR   VEuPathDB; HostDB:ENSG00000197140; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000161015; -.
DR   HOGENOM; CLU_012714_4_3_1; -.
DR   InParanoid; Q8TC27; -.
DR   OMA; GWQCLCP; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q8TC27; -.
DR   TreeFam; TF314733; -.
DR   PathwayCommons; Q8TC27; -.
DR   SignaLink; Q8TC27; -.
DR   BioGRID-ORCS; 203102; 18 hits in 1147 CRISPR screens.
DR   GenomeRNAi; 203102; -.
DR   Pharos; Q8TC27; Tdark.
DR   PRO; PR:Q8TC27; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q8TC27; Protein.
DR   Bgee; ENSG00000197140; Expressed in left testis and 98 other cell types or tissues.
DR   ExpressionAtlas; Q8TC27; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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.
DR   Genevisible; Q8TC27; HS.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   PROPEP          17..174
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000029138"
FT   CHAIN           175..787
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 32"
FT                   /id="PRO_0000029139"
FT   TOPO_DOM        175..682
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        683..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        704..787
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          186..383
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          391..479
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          622..654
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          715..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        772..787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        295..378
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..362
FT                   /evidence="ECO:0000250"
FT   DISULFID        339..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        450..471
FT                   /evidence="ECO:0000250"
FT   DISULFID        626..636
FT                   /evidence="ECO:0000250"
FT   DISULFID        630..642
FT                   /evidence="ECO:0000250"
FT   DISULFID        644..653
FT                   /evidence="ECO:0000250"
FT   VARIANT         98
FT                   /note="Q -> R (in dbSNP:rs17856744)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_055241"
FT   VARIANT         160
FT                   /note="S -> G (in dbSNP:rs17852343)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_055242"
FT   VARIANT         327
FT                   /note="L -> V (in dbSNP:rs9643859)"
FT                   /id="VAR_055243"
FT   VARIANT         467
FT                   /note="T -> S (in dbSNP:rs7845771)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_051591"
FT   VARIANT         658
FT                   /note="K -> N (in dbSNP:rs13277386)"
FT                   /id="VAR_055244"
FT   VARIANT         778
FT                   /note="D -> E (in dbSNP:rs28705715)"
FT                   /id="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
//