ADAM7_HUMAN
ID ADAM7_HUMAN Reviewed; 754 AA.
AC Q9H2U9; A8K8X7; O75959; Q6PEJ6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 7;
DE Short=ADAM 7;
DE AltName: Full=Sperm maturation-related glycoprotein GP-83;
DE Flags: Precursor;
GN Name=ADAM7; Synonyms=GP83;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Epididymis;
RA Lin Y.C., Lee Y.M., Sun G.H., Liu H.W.;
RT "Expression of human ADAM7 (GP-83).";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 167-754 (ISOFORM 1).
RC TISSUE=Epididymis;
RA Liu H.W., Lin Y.C., Sun G.H.;
RT "A ADAM-like cDNA sequence identified in cDNA library of human
RT epididymis.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, INVOLVEMENT IN CUTANEOUS MELANOMA, VARIANTS SER-14;
RP CYS-31; SER-36; TYR-106; PRO-173; ALA-180; TYR-243; GLU-302; ILE-359;
RP GLU-533; LEU-593; LYS-639 AND ASN-703, AND CHARACTERIZATION OF VARIANTS
RP TYR-243; ILE-359; LYS-639 AND ASN-703.
RX PubMed=21618342; DOI=10.1002/humu.21477;
RA Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U.,
RA Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
RT "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and
RT ADAM7 are often mutated in melanoma.";
RL Hum. Mutat. 32:E2148-E2175(2011).
CC -!- FUNCTION: May play an important role in male reproduction including
CC sperm maturation and gonadotrope function. This is a non catalytic
CC metalloprotease-like protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2U9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2U9-2; Sequence=VSP_056602, VSP_056603;
CC -!- TISSUE SPECIFICITY: Not detected in healthy melanocytes. Expressed in
CC melanoma cells. {ECO:0000269|PubMed:21618342}.
CC -!- DISEASE: Note=Has been found to be frequently mutated in melanoma.
CC ADAM7 mutations may play a role in melanoma progression and metastasis.
CC {ECO:0000269|PubMed:21618342}.
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DR EMBL; AF215824; AAG43987.1; -; mRNA.
DR EMBL; AK292492; BAF85181.1; -; mRNA.
DR EMBL; AC024958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058037; AAH58037.1; -; mRNA.
DR EMBL; AF090327; AAC36742.1; -; mRNA.
DR CCDS; CCDS6045.1; -. [Q9H2U9-1]
DR RefSeq; NP_003808.2; NM_003817.3. [Q9H2U9-1]
DR AlphaFoldDB; Q9H2U9; -.
DR SMR; Q9H2U9; -.
DR BioGRID; 114292; 50.
DR STRING; 9606.ENSP00000175238; -.
DR MEROPS; M12.956; -.
DR GlyGen; Q9H2U9; 6 sites.
DR iPTMnet; Q9H2U9; -.
DR PhosphoSitePlus; Q9H2U9; -.
DR SwissPalm; Q9H2U9; -.
DR BioMuta; ADAM7; -.
DR DMDM; 296439449; -.
DR MassIVE; Q9H2U9; -.
DR PaxDb; Q9H2U9; -.
DR PeptideAtlas; Q9H2U9; -.
DR PRIDE; Q9H2U9; -.
DR ProteomicsDB; 67078; -.
DR ProteomicsDB; 80599; -. [Q9H2U9-1]
DR Antibodypedia; 22842; 86 antibodies from 21 providers.
DR DNASU; 8756; -.
DR Ensembl; ENST00000175238.10; ENSP00000175238.5; ENSG00000069206.15. [Q9H2U9-1]
DR Ensembl; ENST00000441335.6; ENSP00000393073.2; ENSG00000069206.15. [Q9H2U9-2]
DR GeneID; 8756; -.
DR KEGG; hsa:8756; -.
DR MANE-Select; ENST00000175238.10; ENSP00000175238.5; NM_003817.4; NP_003808.2.
DR UCSC; uc003xea.2; human. [Q9H2U9-1]
DR CTD; 8756; -.
DR DisGeNET; 8756; -.
DR GeneCards; ADAM7; -.
DR HGNC; HGNC:214; ADAM7.
DR HPA; ENSG00000069206; Tissue enriched (epididymis).
DR MIM; 607310; gene.
DR neXtProt; NX_Q9H2U9; -.
DR OpenTargets; ENSG00000069206; -.
DR PharmGKB; PA24532; -.
DR VEuPathDB; HostDB:ENSG00000069206; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161406; -.
DR HOGENOM; CLU_1309742_0_0_1; -.
DR InParanoid; Q9H2U9; -.
DR OMA; NYSCAEL; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9H2U9; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; Q9H2U9; -.
DR BioGRID-ORCS; 8756; 10 hits in 1068 CRISPR screens.
DR GenomeRNAi; 8756; -.
DR Pharos; Q9H2U9; Tbio.
DR PRO; PR:Q9H2U9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H2U9; protein.
DR Bgee; ENSG00000069206; Expressed in corpus epididymis and 14 other tissues.
DR ExpressionAtlas; Q9H2U9; baseline and differential.
DR Genevisible; Q9H2U9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; 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; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..176
FT /evidence="ECO:0000250"
FT /id="PRO_0000029052"
FT CHAIN 177..754
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 7"
FT /id="PRO_0000029053"
FT TOPO_DOM 19..668
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 199..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..389
FT /evidence="ECO:0000250"
FT DISULFID 350..373
FT /evidence="ECO:0000250"
FT DISULFID 352..357
FT /evidence="ECO:0000250"
FT DISULFID 460..480
FT /evidence="ECO:0000250"
FT VAR_SEQ 194..210
FT /note="GIHDEKYVELFIVADDT -> VSTLLLSLPQMKHLLFS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056602"
FT VAR_SEQ 211..754
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056603"
FT VARIANT 14
FT /note="P -> S (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs150319320)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066296"
FT VARIANT 25
FT /note="E -> Q (in dbSNP:rs34852692)"
FT /id="VAR_046728"
FT VARIANT 31
FT /note="R -> C (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs137990671)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066297"
FT VARIANT 36
FT /note="P -> S (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs267601866)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066298"
FT VARIANT 106
FT /note="H -> Y (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs267601867)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066299"
FT VARIANT 173
FT /note="L -> P (detected in a melanoma cell line)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066300"
FT VARIANT 180
FT /note="V -> A (in a cutaneous metastatic melanoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066301"
FT VARIANT 205
FT /note="I -> V (in dbSNP:rs7829386)"
FT /id="VAR_046729"
FT VARIANT 243
FT /note="H -> Y (in a cutaneous metastatic melanoma sample;
FT somatic mutation; does not affect cell growth but conferes
FT reduced cell adhesion to laminin-1)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066302"
FT VARIANT 244
FT /note="V -> M (in dbSNP:rs13255694)"
FT /id="VAR_046730"
FT VARIANT 302
FT /note="G -> E (in a cutaneous metastatic melanoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066303"
FT VARIANT 359
FT /note="M -> I (in a cutaneous metastatic melanoma sample;
FT somatic mutation; does not affect cell growth but conferes
FT reduced cell adhesion to collagen IV; dbSNP:rs267601868)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066304"
FT VARIANT 453
FT /note="I -> T (in dbSNP:rs3736281)"
FT /id="VAR_046731"
FT VARIANT 533
FT /note="G -> E (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs867202281)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066305"
FT VARIANT 570
FT /note="L -> V (in dbSNP:rs2307044)"
FT /id="VAR_046732"
FT VARIANT 593
FT /note="F -> L (detected in a melanoma cell line)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066306"
FT VARIANT 638
FT /note="N -> H (in dbSNP:rs13259668)"
FT /id="VAR_046733"
FT VARIANT 639
FT /note="E -> K (in a cutaneous metastatic melanoma sample;
FT somatic mutation; does not affect cell growth but conferes
FT reduced cell adhesion to collagen IV and laminin-1;
FT increases cell migration capabilities compared to wild-
FT type; dbSNP:rs1034941983)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066307"
FT VARIANT 703
FT /note="S -> N (in a cutaneous metastatic melanoma sample;
FT somatic mutation; does not affect cell growth but conferes
FT reduced cell adhesion to collagen IV and laminin-1;
FT increases cell migration capabilities compared to wild-
FT type)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066308"
FT VARIANT 735
FT /note="L -> P (in dbSNP:rs6980829)"
FT /id="VAR_046734"
FT CONFLICT 95
FT /note="E -> G (in Ref. 1; AAG43987)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..370
FT /note="KF -> DL (in Ref. 5; AAC36742)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="S -> R (in Ref. 5; AAC36742)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="E -> D (in Ref. 1; AAG43987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 85669 MW; D9E9DF9B5812B0A7 CRC64;
MLPGCIFLMI LLIPQVKEKF ILGVEGQQLV RPKKLPLIQK RDTGHTHDDD ILKTYEEELL
YEIKLNRKTL VLHLLRSREF LGSNYSETFY SMKGEAFTRH PQIMDHCFYQ GSIVHEYDSA
ASISTCNGLR GFFRINDQRY LIEPVKYSDE GEHLVFKYNL RVPYGANYSC TELNFTRKTV
PGDNESEEDS KIKGIHDEKY VELFIVADDT VYRRNGHPHN KLRNRIWGMV NFVNMIYKTL
NIHVTLVGIE IWTHEDKIEL YSNIETTLLR FSFWQEKILK TRKDFDHVVL LSGKWLYSHV
QGISYPGGMC LPYYSTSIIK DLLPDTNIIA NRMAHQLGHN LGMQHDEFPC TCPSGKCVMD
SDGSIPALKF SKCSQNQYHQ YLKDYKPTCM LNIPFPYNFH DFQFCGNKKL DEGEECDCGP
AQECTNPCCD AHTCVLKPGF TCAEGECCES CQIKKAGSIC RPAKDECDFP EMCTGHSPAC
PKDQFRVNGF PCKNSEGYCF MGKCPTREDQ CSELFDDEAI ESHDICYKMN TKGNKFGYCK
NKENRFLPCE EKDVRCGKIY CTGGELSSLL GEDKTYHLKD PQKNATVKCK TIFLYHDSTD
IGLVASGTKC GEGMVCNNGE CLNMEKVYIS TNCPSQCNEN PVDGHGLQCH CEEGQAPVAC
EETLHVTNIT ILVVVLVLVI VGIGVLILLV RYRKCIKLKQ VQSPPTETLG VENKGYFGDE
QQIRTEPILP EIHFLNKPAS KDSRGIADPN QSAK
