ADA32_MOUSE
ID ADA32_MOUSE Reviewed; 754 AA.
AC Q8K410; Q6P901; Q8BJ80;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 32;
DE Short=ADAM 32;
DE Flags: Precursor;
GN Name=Adam32;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-754 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Testis;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in sperm development and fertilization This
CC is a non-catalytic metalloprotease-like protein.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K410-2; Sequence=VSP_012052;
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis and weakly expressed
CC in the epididymis, brain and heart. {ECO:0000269|PubMed:12568724}.
CC -!- DEVELOPMENTAL STAGE: First detected in the testis at day 16 and was
CC reached to the adult level by day 30 after birth.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60983.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN03858.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK005759; BAC25124.1; -; mRNA.
DR EMBL; BC060983; AAH60983.1; ALT_INIT; mRNA.
DR EMBL; AF513715; AAN03858.1; ALT_INIT; mRNA.
DR CCDS; CCDS40300.2; -. [Q8K410-1]
DR CCDS; CCDS80867.1; -. [Q8K410-2]
DR RefSeq; NP_001280622.1; NM_001293693.1. [Q8K410-2]
DR RefSeq; NP_700446.2; NM_153397.2. [Q8K410-1]
DR AlphaFoldDB; Q8K410; -.
DR SMR; Q8K410; -.
DR BioGRID; 237267; 9.
DR STRING; 10090.ENSMUSP00000113627; -.
DR MEROPS; M12.960; -.
DR GlyGen; Q8K410; 5 sites.
DR iPTMnet; Q8K410; -.
DR PhosphoSitePlus; Q8K410; -.
DR PaxDb; Q8K410; -.
DR PRIDE; Q8K410; -.
DR ProteomicsDB; 285664; -. [Q8K410-1]
DR ProteomicsDB; 285665; -. [Q8K410-2]
DR Antibodypedia; 23785; 163 antibodies from 25 providers.
DR DNASU; 353188; -.
DR Ensembl; ENSMUST00000119720; ENSMUSP00000113076; ENSMUSG00000037437. [Q8K410-2]
DR Ensembl; ENSMUST00000121438; ENSMUSP00000113627; ENSMUSG00000037437. [Q8K410-1]
DR GeneID; 353188; -.
DR KEGG; mmu:353188; -.
DR UCSC; uc009lfh.2; mouse. [Q8K410-1]
DR UCSC; uc009lfi.2; mouse. [Q8K410-2]
DR CTD; 203102; -.
DR MGI; MGI:2653822; Adam32.
DR VEuPathDB; HostDB:ENSMUSG00000037437; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161015; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; Q8K410; -.
DR OMA; KPQMQKK; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q8K410; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 353188; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Adam32; mouse.
DR PRO; PR:Q8K410; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K410; protein.
DR Bgee; ENSMUSG00000037437; Expressed in spermatid and 63 other tissues.
DR ExpressionAtlas; Q8K410; baseline and differential.
DR Genevisible; Q8K410; MM.
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; 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..176
FT /evidence="ECO:0000255"
FT /id="PRO_0000029140"
FT CHAIN 177..754
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 32"
FT /id="PRO_0000029141"
FT TOPO_DOM 177..689
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 711..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 187..384
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 391..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 628..660
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 720..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC27"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..379
FT /evidence="ECO:0000250"
FT DISULFID 338..363
FT /evidence="ECO:0000250"
FT DISULFID 340..345
FT /evidence="ECO:0000250"
FT DISULFID 454..475
FT /evidence="ECO:0000250"
FT DISULFID 632..642
FT /evidence="ECO:0000250"
FT DISULFID 636..648
FT /evidence="ECO:0000250"
FT DISULFID 650..659
FT /evidence="ECO:0000250"
FT VAR_SEQ 641..754
FT /note="VCNSHGVCHCNAGYSPPNCQYPTTKRSASLWSGKHDLPMERASKNQEKKWLL
FT SLYIVLIILASVFLIGTGWKGLKQCGSKEEESMSSESKSEDSTYTYVSRSTSETSSMTS
FT TSS -> KQIRRQHLHVCQQVSSLKDGVKRHVENEHHNFQPINF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012052"
FT CONFLICT 361
FT /note="S -> I (in Ref. 3; AAN03858)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="E -> K (in Ref. 2; AAH60983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 83985 MW; 27092719C526934E CRC64;
MLGAMLHTLL LLLLAELGAL LASGPESQSS FLEIIFPEKI EDKTHSEEQI SYIIPINKKQ
YTVHLQKRYF LTNRFMVYMY NQGSTSFHSP NIPAQCYYQG HIKGYPNSVA TLSTCSGLRG
FLQFENVSYG IEPLQSAFTS QHIVYKLGNK EKELIFNKNS RNIEMPTNYG ILINKKPKSP
FKNLFPLYLE MSIVVDKALY DYLGSDSNIV TNKIIEIISL INSVFAQLKV TIVLSSLELW
SDKNKIPTVG EADELLHKFL EWKQAYLTLR PHDVAYLFIY NEYPNYMGAT YPGKMCTAHY
SAGITMYPKD MTLEAFSVIL TQMLGLSLGI SYDEPEKCYC SESICIMNPR AMQYGGVKSF
SNCSLNDFEH FKSNEGAKCL QNKPQMQRTA AAVCGNGKVE GDEICDCGSE AECGPDSCCE
PNRCVLKAGR ACDSKSPSST CCKNCQFLPE KHQCRPEKHL YCDIPEVCNG SSGNCPPDVT
INNGHVCKES GTICYNGDCP DLDRVCESIY GAGSVNAPFA CYEEIQGQND RFGNCGKDNR
NRYVFCGWRN LICGRLICTY PTRMPYNPPN NSTASVIYAF VRDKVCITVD FGSSVKEDPL
RVANGATCDL DRICLNGVCV ESRFLRDQSK TCSSKCHGNG VCNSHGVCHC NAGYSPPNCQ
YPTTKRSASL WSGKHDLPME RASKNQEKKW LLSLYIVLII LASVFLIGTG WKGLKQCGSK
EEESMSSESK SEDSTYTYVS RSTSETSSMT STSS
