ID Q5JRP2_HUMAN Unreviewed; 906 AA.
AC Q5JRP2; U5NE98;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=ADAM metallopeptidase domain 12 {ECO:0000313|Ensembl:ENSP00000391268.2};
DE SubName: Full=Metalloprotease-disintegrin 12 transmembrane isoform La {ECO:0000313|EMBL:AGX93290.1};
GN Name=ADAM12 {ECO:0000313|EMBL:AGX93290.1,
GN ECO:0000313|Ensembl:ENSP00000391268.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000391268.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000391268.2, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2] {ECO:0000313|EMBL:AGX93290.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24116070;
RA Duhachek-Muggy S., Li H., Qi Y., Zolkiewska A.;
RT "Alternative mRNA Splicing Generates Two Distinct ADAM12 Prodomain
RT Variants.";
RL PLoS ONE 8:E75730-E75730(2013).
RN [3] {ECO:0000313|Ensembl:ENSP00000391268.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AC022015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC063963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF444157; AGX93290.1; -; mRNA.
DR RefSeq; NP_001275902.1; NM_001288973.1.
DR MEROPS; M12.212; -.
DR ProteomicsDB; 63102; -.
DR Antibodypedia; 19223; 545 antibodies from 40 providers.
DR DNASU; 8038; -.
DR Ensembl; ENST00000448723.2; ENSP00000391268.2; ENSG00000148848.15.
DR GeneID; 8038; -.
DR MANE-Select; ENST00000448723.2; ENSP00000391268.2; NM_001288973.2; NP_001275902.1.
DR UCSC; uc057wtm.1; human.
DR HGNC; HGNC:190; ADAM12.
DR VEuPathDB; HostDB:ENSG00000148848; -.
DR GeneTree; ENSGT00940000155495; -.
DR HOGENOM; CLU_087486_0_0_1; -.
DR OrthoDB; 5406290at2759; -.
DR BioGRID-ORCS; 8038; 11 hits in 1155 CRISPR screens.
DR ChiTaRS; ADAM12; human.
DR GenomeRNAi; 8038; -.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; ENSG00000148848; Expressed in placenta and 143 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF112; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 12; 1.
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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:AGX93290.1};
KW Integrin {ECO:0000313|EMBL:AGX93290.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000313|EMBL:AGX93290.1};
KW Protease {ECO:0000313|EMBL:AGX93290.1};
KW Proteomics identification {ECO:0007829|MaxQB:Q5JRP2,
KW ECO:0007829|PeptideAtlas:Q5JRP2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..906
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118658"
FT TRANSMEM 705..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..413
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 421..507
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 653..685
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 819..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 479..499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 657..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 675..684
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 906 AA; 99217 MW; 123529DAF0A11D91 CRC64;
MAARPLPVSP ARALLLALAG ALLAPCEARG VSLWNQGRAD EVVSASVGSG DLWIPVKSFD
SKNHPEVLNI RLQRESKELI INLERNEGLI ASSFTETHYL QDGTDVSLAR NYTGHCYYHG
HVRGYSDSAV SLSTCSGLRG LIVFENESYV LEPMKSATNR YKLFPAKKLK SVRGSCGSHH
NTPNLAAKNV FPPPSQTWAR RHKRETLKAT KYVELVIVAD NREFQRQGKD LEKVKQRLIE
IANHVDKFYR PLNIRIVLVG VEVWNDMDKC SVSQDPFTSL HEFLDWRKMK LLPRKSHDNA
QLVSGVYFQG TTIGMAPIMS MCTADQSGGI VMDHSDNPLG AAVTLAHELG HNFGMNHDTL
DRGCSCQMAV EKGGCIMNAS TGYPFPMVFS SCSRKDLETS LEKGMGVCLF NLPEVRESFG
GQKCGNRFVE EGEECDCGEP EECMNRCCNA TTCTLKPDAV CAHGLCCEDC QLKPAGTACR
DSSNSCDLPE FCTGASPHCP ANVYLHDGHS CQDVDGYCYN GICQTHEQQC VTLWGPGAKP
APGICFERVN SAGDPYGNCG KVSKSSFAKC EMRDAKCGKI QCQGGASRPV IGTNAVSIET
NIPLQQGGRI LCRGTHVYLG DDMPDPGLVL AGTKCADGKI CLNRQCQNIS VFGVHECAMQ
CHGRGVCNNR KNCHCEAHWA PPFCDKFGFG GSTDSGPIRQ ADNQGLTIGI LVTILCLLAA
GFVVYLKRKT LIRLLFTNKK TTIEKLRCVR PSRPPRGFQP CQAHLGHLGK GLMRKPPDSY
PPKDNPRRLL QCQNVDISRP LNGLNVPQPQ STQRVLPPLH RAPRAPSVPA RPLPAKPALR
QAQGTCKPNP PQKPLPADPL ARTTRLTHAL ARTPGQWETG LRLAPLRPAP QYPHQVPRST
HTAYIK
//
