ADM1B_MOUSE
ID ADM1B_MOUSE Reviewed; 806 AA.
AC Q8R534; B2RU57; Q9R156;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 1b;
DE Short=ADAM 1b;
DE EC=3.4.24.-;
DE AltName: Full=Fertilin subunit alpha-b;
DE Flags: Precursor;
GN Name=Adam1b;
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:BAB86767.1};
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 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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-331.
RX PubMed=10395895; DOI=10.1016/s0378-1119(99)00208-5;
RA Zhu G.-Z., Lin Y., Myles D.G., Primakoff P.;
RT "Identification of four novel ADAMs with potential roles in spermatogenesis
RT and fertilization.";
RL Gene 234:227-237(1999).
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).
CC -!- FUNCTION: May play a role in spermatogenesis and sperm maturation.
CC {ECO:0000303|PubMed:12095680}.
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 detected 20 days after birth and
CC increases gradually up to day 60. {ECO:0000269|PubMed:12095680}.
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DR EMBL; AB048843; BAB86767.1; -; Genomic_DNA.
DR EMBL; BC140979; AAI40980.1; -; mRNA.
DR EMBL; AF167406; AAD48845.1; -; mRNA.
DR CCDS; CCDS19636.1; -.
DR RefSeq; NP_742123.2; NM_172125.2.
DR AlphaFoldDB; Q8R534; -.
DR SMR; Q8R534; -.
DR BioGRID; 235034; 9.
DR CORUM; Q8R534; -.
DR STRING; 10090.ENSMUSP00000078343; -.
DR MEROPS; M12.203; -.
DR GlyGen; Q8R534; 6 sites.
DR iPTMnet; Q8R534; -.
DR PhosphoSitePlus; Q8R534; -.
DR PaxDb; Q8R534; -.
DR PRIDE; Q8R534; -.
DR ProteomicsDB; 296111; -.
DR DNASU; 280667; -.
DR Ensembl; ENSMUST00000079368; ENSMUSP00000078343; ENSMUSG00000062438.
DR GeneID; 280667; -.
DR KEGG; mmu:280667; -.
DR UCSC; uc008zjn.1; mouse.
DR CTD; 100420505; -.
DR MGI; MGI:2429506; Adam1b.
DR VEuPathDB; HostDB:ENSMUSG00000062438; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161891; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; Q8R534; -.
DR OMA; HTLIQVP; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q8R534; -.
DR TreeFam; TF314733; -.
DR BRENDA; 3.4.24.B8; 3474.
DR BioGRID-ORCS; 280667; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Adam1b; mouse.
DR PRO; PR:Q8R534; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R534; protein.
DR Bgee; ENSMUSG00000062438; Expressed in spermatid and 5 other tissues.
DR Genevisible; Q8R534; MM.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; 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; 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein 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..33
FT /evidence="ECO:0000255"
FT PROPEP 34..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000029034"
FT CHAIN ?..806
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 1b"
FT /id="PRO_0000029035"
FT TOPO_DOM ?..704
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 726..806
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 406..490
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 631..665
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..392
FT /evidence="ECO:0000250"
FT DISULFID 353..376
FT /evidence="ECO:0000250"
FT DISULFID 355..361
FT /evidence="ECO:0000250"
FT DISULFID 462..482
FT /evidence="ECO:0000250"
FT DISULFID 635..647
FT /evidence="ECO:0000255"
FT DISULFID 641..653
FT /evidence="ECO:0000255"
FT DISULFID 655..664
FT /evidence="ECO:0000255"
FT CONFLICT 363
FT /note="M -> R (in Ref. 1; BAB86767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 89369 MW; 5DD6EFA9B595B43D CRC64;
MERLKLGKIP EHWCIRLVAM LLLAIIFLPS TFCDIGSVYN SSYETVIPER LPGKGGKDPG
GKVSYMLLMQ GQKQLLHLEV KGHYPENNFP VYSYHNGILR QEMPLLSQDC HYEGYMEGVP
GSFVSVNICS GLRGVLIKEE TSYGIEPMLS SKNFEHVLYT MEHQPVVSCS VTPKDSPGDT
SHPPRSRKPD DLLVLTDWWS HTKYVEMFVV VNHQRFQMWG SNINETVQAV MDIIALANSF
TRGINTEVVL VGLEIWTEGD PIEVPVDLQT TLRNFNFWRQ EKLVGRVRHD VAHLIVGHRP
GENEGQAFLR GACSGEFAAA VEAFHHEDVL LFAALMAHEL GHNLGIQHDH PTCTCGPKHF
CLMGEKIGKD SGFSNCSSDH FLRFLHDHRG VCLLDEPGRQ SRMRRAANCG NGVVEDLEQC
DCGSDCDKSQ CCDENCKLKG NSVCSTELCC FKCNFKKEGD VCRPADGPCD LEEYCNGTSA
ACPSDRKAQD GSKCHESFLC FNGQCMDPTF QCSRIFGHGS RSASDYCYTS LNSRGDQFGN
CGSSSQFPKK YTKCSDKNVM CGKLICTEVA FLPQIQPNNL LLQVPETEDW CWSVAVFDMR
DSLHEEYVKD NTYCGKDKVC KNSICEDFTP FSFPCSPSKQ CNKHGVCNDL GNCHCSFGFA
PPDCKEEGTG GSVDSGPAVN LSNDSSPGPN STQSSTEELI LNLKLIVLAV ILVLMILLII
ICIISAYTKS ETASEAGPSE LEELPEGEKE EQEEVLPEEA KGEEEELEYG KEEAEEQGAV
EEEGAEEANE EAAAEKKDED EEEGEE
