GenomeNet

Database: UniProt
Entry: Q3TTE0
LinkDB: Q3TTE0
Original site: Q3TTE0 
ID   ADAM5_MOUSE             Reviewed;         751 AA.
AC   Q3TTE0; Q3TTE2; Q52KQ5; Q60623; Q60816; Q8CDV5; Q9D4F0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   10-APR-2019, entry version 108.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 5;
DE   AltName: Full=Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein II;
DE            Short=tMDC II;
DE   Flags: Precursor;
GN   Name=Adam5; Synonyms=Tmdc2;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=7750654; DOI=10.1006/dbio.1995.1152;
RA   Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.-P.,
RA   Primakoff P., Myles D.G., White J.M.;
RT   "ADAM, a widely distributed and developmentally regulated gene family
RT   encoding membrane proteins with a disintegrin and metalloprotease
RT   domain.";
RL   Dev. Biol. 169:378-383(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   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).
RN   [5]
RP   INTERACTION WITH TEX101.
RX   PubMed=23969891; DOI=10.1093/jmcb/mjt031;
RA   Li W., Guo X.J., Teng F., Hou X.J., Lv Z., Zhou S.Y., Bi Y., Wan H.F.,
RA   Feng C.J., Yuan Y., Zhao X.Y., Wang L., Sha J.H., Zhou Q.;
RT   "Tex101 is essential for male fertility by affecting sperm migration
RT   into the oviduct in mice.";
RL   J. Mol. Cell Biol. 5:345-347(2013).
CC   -!- FUNCTION: This is a non catalytic metalloprotease-like protein.
CC       May play a role in sperm-egg fusion (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TEX101. {ECO:0000269|PubMed:23969891}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3TTE0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TTE0-2; Sequence=VSP_035338;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q3TTE0-3; Sequence=VSP_035334, VSP_035337;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q3TTE0-4; Sequence=VSP_035335, VSP_035336;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Detected in brain, kidney, liver, lung, spleen
CC       and ovary. Highly expressed in testis.
CC       {ECO:0000269|PubMed:7750654}.
CC   -!- PTM: Subject to proteolytic processing during epididymal transit
CC       of spermatozoa. {ECO:0000250}.
CC   -!- CAUTION: Not expected to have protease activity. {ECO:0000305}.
DR   EMBL; U22059; AAA74923.1; -; mRNA.
DR   EMBL; AK016574; BAB30315.1; -; mRNA.
DR   EMBL; AK029519; BAC26490.1; -; mRNA.
DR   EMBL; AK161262; BAE36276.1; -; mRNA.
DR   EMBL; AK161415; BAE36383.1; -; mRNA.
DR   EMBL; AK161417; BAE36385.1; -; mRNA.
DR   EMBL; BC094237; AAH94237.1; -; mRNA.
DR   CCDS; CCDS52525.1; -. [Q3TTE0-1]
DR   CCDS; CCDS72107.1; -. [Q3TTE0-2]
DR   CCDS; CCDS85515.1; -. [Q3TTE0-3]
DR   PIR; I48948; I48948.
DR   RefSeq; NP_001258986.1; NM_001272057.1. [Q3TTE0-3]
DR   RefSeq; NP_001258987.1; NM_001272058.1. [Q3TTE0-2]
DR   RefSeq; NP_001258988.1; NM_001272059.1. [Q3TTE0-4]
DR   RefSeq; NP_031427.2; NM_007401.3. [Q3TTE0-1]
DR   UniGene; Mm.143889; -.
DR   ProteinModelPortal; Q3TTE0; -.
DR   STRING; 10090.ENSMUSP00000112422; -.
DR   MEROPS; M12.953; -.
DR   PaxDb; Q3TTE0; -.
DR   PRIDE; Q3TTE0; -.
DR   Ensembl; ENSMUST00000050300; ENSMUSP00000052661; ENSMUSG00000031554. [Q3TTE0-2]
DR   Ensembl; ENSMUST00000118419; ENSMUSP00000112422; ENSMUSG00000031554. [Q3TTE0-1]
DR   Ensembl; ENSMUST00000209935; ENSMUSP00000147290; ENSMUSG00000031554. [Q3TTE0-3]
DR   GeneID; 11499; -.
DR   KEGG; mmu:11499; -.
DR   UCSC; uc009lff.1; mouse. [Q3TTE0-2]
DR   UCSC; uc009lfg.2; mouse. [Q3TTE0-1]
DR   UCSC; uc012gbm.2; mouse. [Q3TTE0-4]
DR   UCSC; uc012gbn.2; mouse. [Q3TTE0-3]
DR   CTD; 255926; -.
DR   MGI; MGI:104730; Adam5.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000162784; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q3TTE0; -.
DR   OMA; KNLFDYM; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q3TTE0; -.
DR   TreeFam; TF314733; -.
DR   PRO; PR:Q3TTE0; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000031554; Expressed in 47 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q3TTE0; baseline and differential.
DR   Genevisible; Q3TTE0; 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; 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   Alternative splicing; Complete proteome; Disulfide bond;
KW   EGF-like domain; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17    142       {ECO:0000255}.
FT                                /FTId=PRO_0000349301.
FT   CHAIN       143    751       Disintegrin and metalloproteinase domain-
FT                                containing protein 5.
FT                                /FTId=PRO_0000349300.
FT   TOPO_DOM     17    691       Extracellular. {ECO:0000255}.
FT   TRANSMEM    692    712       Helical. {ECO:0000255}.
FT   TOPO_DOM    713    751       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      185    378       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      388    476       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      623    657       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS      3     11       Poly-Leu.
FT   DISULFID    291    373       {ECO:0000250}.
FT   DISULFID    332    357       {ECO:0000250}.
FT   DISULFID    334    339       {ECO:0000250}.
FT   DISULFID    448    468       {ECO:0000250}.
FT   DISULFID    627    639       {ECO:0000250}.
FT   DISULFID    633    645       {ECO:0000250}.
FT   DISULFID    647    656       {ECO:0000250}.
FT   VAR_SEQ     676    699       DGKSYKQQSHSNLKKNQLQLILYI -> APPTNQVLLPQKK
FT                                IIWINHEKLTF (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035334.
FT   VAR_SEQ     676    695       DGKSYKQQSHSNLKKNQLQL -> AHLRTHQSHQTQKGFCT
FT                                SLL (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_035335.
FT   VAR_SEQ     696    751       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_035336.
FT   VAR_SEQ     700    751       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035337.
FT   VAR_SEQ     749    751       TSH -> SSTDPPITPNPERILYVFALKKH (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_035338.
FT   CONFLICT     26     26       Q -> P (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
FT   CONFLICT     29     29       V -> E (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
FT   CONFLICT    346    346       I -> K (in Ref. 2; BAE36383).
FT                                {ECO:0000305}.
FT   CONFLICT    457    458       FV -> LL (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
FT   CONFLICT    470    475       PNTYAR -> LTHMHA (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
FT   CONFLICT    501    501       S -> I (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       R -> T (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
FT   CONFLICT    596    597       TF -> NI (in Ref. 1; AAA74923).
FT                                {ECO:0000305}.
SQ   SEQUENCE   751 AA;  84534 MW;  32043977EA718760 CRC64;
     MFLLLLLFLH LKGLQAGQNP QKTTLQTTVP EKISSPDVET DAEDHMAYLI TINETPHFIH
     LKKQSFITPT AVVYTYDRND VQHSQPLSAL ENCNYNGYVA GFPNSIVTLT VCTGLRGIIQ
     FENVSYAIEP VETLSGFVHV IYENTNKHAV IPDLGKNQSY SWFDESDYQF RSNMKKSGFT
     VLRQRFIMMD IIVDKKLFDY MGSDTEVVLQ KVIQIIGFVN TMLSKLKLTV LINSIEIWSK
     ENRIRLSKAV DDLLVQFSIW KHEYRSQHVA YLLAFEEHPA STGALYPGNL CKLEYNAAVA
     LYPKGLSLES FSVIVLQLLS IGMGLTYDTE NCHCTGEVCL MTPKAIYSGG VKDFSTCTLD
     DFKYLSTRQD LRCLQDLPLE RKPARRPRRI CGNGILEMNE QCDCGTLKNC THRKCCDPMS
     CRLKNKATCG SGECCSQDCT VKMNDVVCRK SVDECDFVEY CNGKDPYCVP NTYARNGQYC
     ESGEAFCFEG RCQTADKQCM SMLGKYVRGA SFACYEEFNS RGDRFGNCIH NFCAFRNSLC
     GKLICTWPFK KLVLKANLSV AYAQIRDDLC VAMYKGGRIP KTTKTTYSNP ADRDETFVND
     GTICGPDMFC LRASCTETRF HMDSSKCDST RDCNDHGVCN NLQHCHCDIG YNPPFCEEHK
     GQFGSVDDGH KYHVEDGKSY KQQSHSNLKK NQLQLILYIS LPLLVMISAV VIKQSKLSRV
     CDRERSESDS STTEDSGSNT NVTSSGGSTS H
//
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