ADM1A_MOUSE
ID ADM1A_MOUSE Reviewed; 791 AA.
AC Q60813; Q60617; Q80WR7; Q8R533;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 1a;
DE Short=ADAM 1a;
DE EC=3.4.24.-;
DE AltName: Full=Fertilin subunit alpha-a;
DE Flags: Precursor;
GN Name=Adam1a; Synonyms=Adam1, Ftna;
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 {ECO:0000312|EMBL:BAB86768.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12095680; DOI=10.1016/s0378-1119(02)00540-1;
RA Nishimura H., Kim E., Fujimori T., Kashiwabara S., Kuroiwa A., Matsuda Y.,
RA Baba T.;
RT "The ADAM1a and ADAM1b genes, instead of the ADAM1 (fertilin alpha) gene,
RT are localized on mouse chromosome 5.";
RL Gene 291:67-76(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 192-791.
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 [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 456-499.
RC STRAIN=BALB/cJ;
RX PubMed=8146185; DOI=10.1073/pnas.91.7.2748;
RA Weskamp G., Blobel C.P.;
RT "A family of cellular proteins related to snake venom disintegrins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2748-2751(1994).
CC -!- FUNCTION: May be involved in sperm-egg fusion.
CC {ECO:0000269|PubMed:8146185}.
CC -!- SUBUNIT: Heterodimer with ADAM2/fertilin subunit beta.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:12095680}.
CC -!- DEVELOPMENTAL STAGE: Expression is low at 20, 22 and 24 days after
CC birth but has increased by day 60. {ECO:0000269|PubMed:12095680}.
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DR EMBL; AB048844; BAB86768.1; -; Genomic_DNA.
DR EMBL; BC052093; AAH52093.1; -; mRNA.
DR EMBL; U22056; AAA74920.1; -; mRNA.
DR EMBL; U06144; AAA18423.1; -; mRNA.
DR CCDS; CCDS19637.1; -.
DR PIR; I48942; I48942.
DR RefSeq; NP_742124.2; NM_172126.2.
DR AlphaFoldDB; Q60813; -.
DR SMR; Q60813; -.
DR CORUM; Q60813; -.
DR STRING; 10090.ENSMUSP00000098320; -.
DR MEROPS; M12.202; -.
DR GlyGen; Q60813; 5 sites.
DR iPTMnet; Q60813; -.
DR PhosphoSitePlus; Q60813; -.
DR PaxDb; Q60813; -.
DR PRIDE; Q60813; -.
DR ProteomicsDB; 285727; -.
DR DNASU; 280668; -.
DR Ensembl; ENSMUST00000100757; ENSMUSP00000098320; ENSMUSG00000072647.
DR GeneID; 280668; -.
DR KEGG; mmu:280668; -.
DR UCSC; uc008zjo.1; mouse.
DR CTD; 8759; -.
DR MGI; MGI:2429504; Adam1a.
DR VEuPathDB; HostDB:ENSMUSG00000072647; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161891; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; Q60813; -.
DR OMA; CAPEKIC; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q60813; -.
DR TreeFam; TF314733; -.
DR BRENDA; 3.4.24.B8; 3474.
DR BioGRID-ORCS; 280668; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Adam1b; mouse.
DR PRO; PR:Q60813; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q60813; protein.
DR Bgee; ENSMUSG00000072647; Expressed in spermatid and 60 other tissues.
DR ExpressionAtlas; Q60813; baseline and differential.
DR Genevisible; Q60813; MM.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; NAS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; NAS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
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 PRINTS; PR00289; DISINTEGRIN.
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.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..65
FT /evidence="ECO:0000255"
FT PROPEP 66..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000029032"
FT CHAIN ?..791
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 1a"
FT /id="PRO_0000029033"
FT TOPO_DOM ?..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..791
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 235..429
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 438..522
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 663..697
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 345..424
FT /evidence="ECO:0000250"
FT DISULFID 385..408
FT /evidence="ECO:0000250"
FT DISULFID 387..393
FT /evidence="ECO:0000250"
FT DISULFID 494..514
FT /evidence="ECO:0000250"
FT DISULFID 667..679
FT /evidence="ECO:0000255"
FT DISULFID 673..685
FT /evidence="ECO:0000255"
FT DISULFID 687..696
FT /evidence="ECO:0000255"
FT CONFLICT 117
FT /note="P -> S (in Ref. 1; BAB86768)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="T -> A (in Ref. 3; AAA74920)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="M -> R (in Ref. 1; BAB86768)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="Y -> I (in Ref. 3; AAA74920)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="T -> S (in Ref. 3; AAA74920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 791 AA; 87490 MW; 0D36DD0D914A39AF CRC64;
MSVAAAGRGF ASSLSSPQIR RIALKEAKLT PHIWAALHWN LGLRLVPSVR VGILVLLIFL
PSTFCDIGSV YNSSYETVIP ERLPGKGGKD PGGKVSYMLL MQGQKQLLHL EVKGHYPENN
FPVYSYHNGI LRQEMPLLSQ DCHYEGYMEG VPGSFVSVNI CSGLRGVLIK EETSYGIEPM
LSSKNFEHVL YTMEHQPVVS CSVTPKDSPG DTSHPPRSRK PDDLLVLTDW WSHTKYVEMF
VVVNHQRFQM WGSNINETVQ AVMDIIALAN SFTRGINTEV VLVGLEIWTE GDPIEVPVDL
QTTLRNFNFW RQEKLVGRVR HDVAHLIVGH RPGENEGQAF LRGACSGEFA AAVEAFHHED
VLLFAALMAH ELGHNLGIQH DHPTCTCGPK HFCLMGEKIG KDSGFSNCSS DHFLRFLHDH
RGACLLDEPG RQSRMRRAAN CGNGVVEDLE ECDCGSDCDS HPCCSPTCTL KEGAQCSEGL
CCYNCTFKKK GSLCRPAEDV CDLPEYCDGS TQECPANSYM QDGTQCDRIY YCLGGWCKNP
DKQCSRIYGY PARSAPEECY ISVNTKANRF GNCGHPTSAN FRYETCSDED VFCGKLVCTD
VRYLPKVKPL HSLLQVPYGE DWCWSMDAYN ITDVPDDGDV QSGTFCAPNK VCMEYICTGR
GVLQYNCEPQ EMCHGNGVCN NFKHCHCDAG FAPPDCSSPG NGGSVDSGPV GKPADRHLSL
SFLAEESPDD KMEDEEVNLK VMVLVVPIFL VVLLCCLMLI AYLWSEVQEV VSPPSSSESS
SSSSWSDSDS Q
