ADAM3_MOUSE
ID ADAM3_MOUSE Reviewed; 822 AA.
AC F8VQ03;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=A disintegrin and metallopeptidase domain 3 {ECO:0000312|MGI:MGI:102518};
DE AltName: Full=Cyritestin {ECO:0000312|MGI:MGI:102518};
DE Flags: Precursor;
GN Name=Adam3 {ECO:0000312|MGI:MGI:102518};
GN Synonyms=Cyrn1 {ECO:0000312|MGI:MGI:102518};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP CHARACTERIZATION.
RX PubMed=11439107; DOI=10.1042/0264-6021:3570551;
RA Grzmil P., Kim Y., Shamsadin R., Neesen J., Adham I.M., Heinlein U.A.,
RA Schwarzer U.J., Engel W.;
RT "Human cyritestin genes (CYRN1 and CYRN2) are non-functional.";
RL Biochem. J. 357:551-556(2001).
RN [3]
RP SUBCELLULAR LOCATION, AND PROCESSING.
RX PubMed=15514464; DOI=10.1262/jrd.50.571;
RA Kim E., Nishimura H., Iwase S., Yamagata K., Kashiwabara S., Baba T.;
RT "Synthesis, processing, and subcellular localization of mouse ADAM3 during
RT spermatogenesis and epididymal sperm transport.";
RL J. Reprod. Dev. 50:571-578(2004).
RN [4]
RP FUNCTION.
RX PubMed=19339711; DOI=10.1095/biolreprod.108.074021;
RA Yamaguchi R., Muro Y., Isotani A., Tokuhiro K., Takumi K., Adham I.,
RA Ikawa M., Okabe M.;
RT "Disruption of ADAM3 impairs the migration of sperm into oviduct in
RT mouse.";
RL Biol. Reprod. 81:142-146(2009).
RN [5]
RP INTERACTION WITH TEX101.
RX PubMed=23633567; DOI=10.1073/pnas.1222166110;
RA Fujihara Y., Tokuhiro K., Muro Y., Kondoh G., Araki Y., Ikawa M., Okabe M.;
RT "Expression of TEX101, regulated by ACE, is essential for the production of
RT fertile mouse spermatozoa.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:8111-8116(2013).
RN [6]
RP INTERACTION WITH LY6K, AND PROCESSING.
RX PubMed=24501175; DOI=10.1095/biolreprod.113.112888;
RA Fujihara Y., Okabe M., Ikawa M.;
RT "GPI-anchored protein complex, LY6K/TEX101, is required for sperm migration
RT into the oviduct and male fertility in mice.";
RL Biol. Reprod. 90:60-60(2014).
CC -!- FUNCTION: Involved in fertilization by controlling sperm migration into
CC oviduct. {ECO:0000269|PubMed:19339711}.
CC -!- SUBUNIT: Interacts with LY6K (PubMed:24501175). Interacts with TEX101
CC (PubMed:23633567). {ECO:0000269|PubMed:23633567,
CC ECO:0000269|PubMed:24501175}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15514464};
CC Single-pass membrane protein {ECO:0000255}. Note=Localized in round and
CC elongating spermatids. Localized on the anterior part of the sperm
CC head, and is removed during the acrosome reaction.
CC {ECO:0000269|PubMed:15514464}.
CC -!- PTM: Initially synthesized as a 110-kDa precursor in round spermatids,
CC and the precursor is then processed into a 42-kDa mature protein during
CC the sperm transport into and/or once in the epididymis.
CC {ECO:0000269|PubMed:15514464, ECO:0000269|PubMed:24501175}.
CC -!- CAUTION: There are two genes in human, ADAM3A and ADAM3B that are non-
CC functional (PubMed:11439107). ADAM3A gene is deleted in infertile men
CC and in some fertile men. ADAM3B transcripts, from testicular RNA of
CC ADAM3A-deficient men, present many stop codons in all possible reading
CC frames. Moreover these two proteins are neither detected in extracts
CC from the testis of a man with the ADAM3A-positive genotype, nor of a
CC man with a ADAM3A-deficient genotype. {ECO:0000305|PubMed:11439107}.
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DR EMBL; AC138355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS22196.1; -.
DR RefSeq; NP_033749.2; NM_009619.5.
DR AlphaFoldDB; F8VQ03; -.
DR SMR; F8VQ03; -.
DR STRING; 10090.ENSMUSP00000033958; -.
DR MaxQB; F8VQ03; -.
DR PaxDb; F8VQ03; -.
DR PRIDE; F8VQ03; -.
DR ProteomicsDB; 285615; -.
DR DNASU; 11497; -.
DR Ensembl; ENSMUST00000033958; ENSMUSP00000033958; ENSMUSG00000031553.
DR Ensembl; ENSMUST00000171438; ENSMUSP00000132651; ENSMUSG00000031553.
DR GeneID; 11497; -.
DR KEGG; mmu:11497; -.
DR UCSC; uc009lfc.1; mouse.
DR CTD; 11497; -.
DR MGI; MGI:102518; Adam3.
DR VEuPathDB; HostDB:ENSMUSG00000031553; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162466; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; F8VQ03; -.
DR OMA; YMGSAVA; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; F8VQ03; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 11497; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adam3; mouse.
DR PRO; PR:F8VQ03; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; F8VQ03; protein.
DR Bgee; ENSMUSG00000031553; Expressed in spermatid and 18 other tissues.
DR ExpressionAtlas; F8VQ03; baseline and differential.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0061827; C:sperm head; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0050684; P:regulation of mRNA processing; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IGI:MGI.
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; IPR013111; EGF_extracell.
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; PF07974; EGF_2; 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 Cell membrane; Disulfide bond; EGF-like domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..822
FT /note="A disintegrin and metallopeptidase domain 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5010674208"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 187..384
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 395..484
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 619..653
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 296..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 338..363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 340..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 456..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 623..635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 629..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 643..652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 822 AA; 91444 MW; C38E63DC72558094 CRC64;
MLPLFLVLSY LGQVIAAGKD VETPLLQITV PEKIDTNIQD AKEAETQVTY VVRIEGKAYT
LQLEKQSFLH PLFGTYLRDK LGTLQPYFSL VKTHCFYQGH AAEIPVSTVT LSTCSGLRGL
LQLENITYGI EPLESSATFE HILYEIKNNK IDYSPLKENF ANSEQESQSY RILVKPEKGS
NSTLTKRILR IKIIMDKAMF DHMGSEVGVA TQKVVHIFGL INTMFSQLKM TVMLNSLEIW
SEQDKIETNG DADEVLQRFL LWKSKEISQK AQDITYLLLY KDHPDYVGAT YHGMACNPNF
TAGIALHPKT LAVEGFAIVL SQLLGINLGL AYDDVYNCFC PGSTCIMNPS AIRSQGIKVF
SSCSVDEFKQ LASQPELDCL RNTSETEFVV QPQGGSYCGN HLLEVPEQCD CGPPETCTHK
KCCNPKDCTL IDAAQCGTGP CCDKRTCTIA ERGRLCRKSK DQCDFPEFCN GETEGCAPDT
KAADLEPCNN ETAYCFGGVC RDPDRQCTDL FGKYAKGPNY VCAQEVNLQN DKFGNCHGRC
NYSAIFCGKA VCYWNFAEVI QTEKYDVQYT YLGGQVCVSA HLRSQTGTRD DTYVHDGTVC
GSGQVCFRGD CLRVHVLRGT RECEADDKCQ GHGICNNLNN CQCESGFAPP ECDMTPSSPG
GSMDDGFWLP FDKSTPLIFK RHGLKYKKVL LISFYILLPF LVVLAFMAVK RMIGKRLAKQ
NISKALEHKE EAFNRGSMNP GVVSGGNTDQ NLMTVPGSFN SYAYHGNTDQ NFMTVPGSFN
SYSYHGNTDQ NFMTVPGSFN SYSYQDVPYY RSIPEDGNDS QQ
