ADA32_HUMAN
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 03-AUG-2022, entry version 161.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 GlyGen; Q8TC27; 4 sites.
DR iPTMnet; Q8TC27; -.
DR PhosphoSitePlus; Q8TC27; -.
DR BioMuta; ADAM32; -.
DR DMDM; 296434389; -.
DR EPD; Q8TC27; -.
DR MassIVE; Q8TC27; -.
DR PaxDb; Q8TC27; -.
DR PeptideAtlas; Q8TC27; -.
DR PRIDE; Q8TC27; -.
DR ProteomicsDB; 74084; -.
DR Antibodypedia; 23785; 163 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 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; KPQMQKK; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q8TC27; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; Q8TC27; -.
DR SignaLink; Q8TC27; -.
DR BioGRID-ORCS; 203102; 18 hits in 1071 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 96 other tissues.
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 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:0006508; P:proteolysis; 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; 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 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
