GenomeNet

Database: UniProt
Entry: Q8K410
LinkDB: Q8K410
Original site: Q8K410 
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   13-FEB-2019, entry version 129.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RP   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
RT   gene 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play a role in sperm development and fertilization
CC       This 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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the testis and weakly
CC       expressed in the epididymis, brain and heart.
CC       {ECO:0000269|PubMed:12568724}.
CC   -!- DEVELOPMENTAL STAGE: First detected in the testis at day 16 and
CC       was reached to the adult level by day 30 after birth.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60983.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAN03858.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Mm.269223; -.
DR   ProteinModelPortal; Q8K410; -.
DR   SMR; Q8K410; -.
DR   BioGrid; 237267; 1.
DR   STRING; 10090.ENSMUSP00000113627; -.
DR   MEROPS; M12.960; -.
DR   iPTMnet; Q8K410; -.
DR   PhosphoSitePlus; Q8K410; -.
DR   PaxDb; Q8K410; -.
DR   PRIDE; Q8K410; -.
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   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000161015; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q8K410; -.
DR   KO; K16070; -.
DR   OMA; SVIVTQM; -.
DR   OrthoDB; 162519at2759; -.
DR   TreeFam; TF314733; -.
DR   PRO; PR:Q8K410; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000037437; Expressed in 36 organ(s), highest expression level in testis.
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   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; 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; 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;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23    176       {ECO:0000255}.
FT                                /FTId=PRO_0000029140.
FT   CHAIN       177    754       Disintegrin and metalloproteinase domain-
FT                                containing protein 32.
FT                                /FTId=PRO_0000029141.
FT   TOPO_DOM    177    689       Extracellular. {ECO:0000255}.
FT   TRANSMEM    690    710       Helical. {ECO:0000255}.
FT   TOPO_DOM    711    754       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      187    384       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      391    483       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      628    660       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    484    506       Cys-rich.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8TC27}.
FT   CARBOHYD    126    126       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    362    362       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    469    469       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    570    570       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    296    379       {ECO:0000250}.
FT   DISULFID    338    363       {ECO:0000250}.
FT   DISULFID    340    345       {ECO:0000250}.
FT   DISULFID    454    475       {ECO:0000250}.
FT   DISULFID    632    642       {ECO:0000250}.
FT   DISULFID    636    648       {ECO:0000250}.
FT   DISULFID    650    659       {ECO:0000250}.
FT   VAR_SEQ     641    754       VCNSHGVCHCNAGYSPPNCQYPTTKRSASLWSGKHDLPMER
FT                                ASKNQEKKWLLSLYIVLIILASVFLIGTGWKGLKQCGSKEE
FT                                ESMSSESKSEDSTYTYVSRSTSETSSMTSTSS -> KQIRR
FT                                QHLHVCQQVSSLKDGVKRHVENEHHNFQPINF (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_012052.
FT   CONFLICT    361    361       S -> I (in Ref. 3; AAN03858).
FT                                {ECO:0000305}.
FT   CONFLICT    728    728       E -> K (in Ref. 2; AAH60983).
FT                                {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
//
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