ADAM5_MOUSE
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 03-AUG-2022, entry version 122.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Primakoff P.,
RA 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 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., 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 [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 project:
RT 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 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 into
RT the oviduct in mice.";
RL J. Mol. Cell Biol. 5:345-347(2013).
CC -!- FUNCTION: This is a non catalytic metalloprotease-like protein. May
CC play a role in sperm-egg fusion (By similarity). {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 Name=3;
CC IsoId=Q3TTE0-3; Sequence=VSP_035334, VSP_035337;
CC Name=4;
CC IsoId=Q3TTE0-4; Sequence=VSP_035335, VSP_035336;
CC -!- TISSUE SPECIFICITY: Detected in brain, kidney, liver, lung, spleen and
CC ovary. Highly expressed in testis. {ECO:0000269|PubMed:7750654}.
CC -!- PTM: Subject to proteolytic processing during epididymal transit of
CC spermatozoa. {ECO:0000250}.
CC -!- CAUTION: Not expected to have protease activity. {ECO:0000305}.
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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 AlphaFoldDB; Q3TTE0; -.
DR SMR; Q3TTE0; -.
DR BioGRID; 197970; 9.
DR STRING; 10090.ENSMUSP00000112422; -.
DR MEROPS; M12.953; -.
DR PaxDb; Q3TTE0; -.
DR PRIDE; Q3TTE0; -.
DR ProteomicsDB; 285671; -. [Q3TTE0-1]
DR ProteomicsDB; 285672; -. [Q3TTE0-2]
DR ProteomicsDB; 285673; -. [Q3TTE0-3]
DR ProteomicsDB; 285674; -. [Q3TTE0-4]
DR DNASU; 11499; -.
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 VEuPathDB; HostDB:ENSMUSG00000031554; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162784; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; Q3TTE0; -.
DR OMA; KNLFDYM; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q3TTE0; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 11499; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Adam5; mouse.
DR PRO; PR:Q3TTE0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TTE0; protein.
DR Bgee; ENSMUSG00000031554; Expressed in spermatid and 28 other tissues.
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 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 Alternative splicing; Disulfide bond; EGF-like domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..142
FT /evidence="ECO:0000255"
FT /id="PRO_0000349301"
FT CHAIN 143..751
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 5"
FT /id="PRO_0000349300"
FT TOPO_DOM 17..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 185..378
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 388..476
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 623..657
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 722..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 291..373
FT /evidence="ECO:0000250"
FT DISULFID 332..357
FT /evidence="ECO:0000250"
FT DISULFID 334..339
FT /evidence="ECO:0000250"
FT DISULFID 448..468
FT /evidence="ECO:0000250"
FT DISULFID 627..639
FT /evidence="ECO:0000250"
FT DISULFID 633..645
FT /evidence="ECO:0000250"
FT DISULFID 647..656
FT /evidence="ECO:0000250"
FT VAR_SEQ 676..699
FT /note="DGKSYKQQSHSNLKKNQLQLILYI -> APPTNQVLLPQKKIIWINHEKLTF
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035334"
FT VAR_SEQ 676..695
FT /note="DGKSYKQQSHSNLKKNQLQL -> AHLRTHQSHQTQKGFCTSLL (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035335"
FT VAR_SEQ 696..751
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035336"
FT VAR_SEQ 700..751
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035337"
FT VAR_SEQ 749..751
FT /note="TSH -> SSTDPPITPNPERILYVFALKKH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035338"
FT CONFLICT 26
FT /note="Q -> P (in Ref. 1; AAA74923)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="V -> E (in Ref. 1; AAA74923)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="I -> K (in Ref. 2; BAE36383)"
FT /evidence="ECO:0000305"
FT CONFLICT 457..458
FT /note="FV -> LL (in Ref. 1; AAA74923)"
FT /evidence="ECO:0000305"
FT CONFLICT 470..475
FT /note="PNTYAR -> LTHMHA (in Ref. 1; AAA74923)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="S -> I (in Ref. 1; AAA74923)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="R -> T (in Ref. 1; AAA74923)"
FT /evidence="ECO:0000305"
FT CONFLICT 596..597
FT /note="TF -> NI (in Ref. 1; AAA74923)"
FT /evidence="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
