(data stored in ACNUC30567 zone)

HOGENOM: HS8_PE1198

ID   HS8_PE1198                           STANDARD;      PRT;   739 AA.
AC   HS8_PE1198; Q9Y3Q7; B2R9Y0; Q0VAI4; Q6UXJ9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein
DE   18; Short=ADAM 18;AltName: Full=Transmembrane metalloproteinase-like,
DE   disintegrin-like, and cysteine-rich protein III; Short=tMDC III;Flags:
DE   Precursor; (HS8.PE1198).
GN   Name=ADAM18; Synonyms=TMDC3; ORFNames=UNQ858/PRO1867;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS8.PE1198.
CC       Homo sapiens chromosome 8 GRCh37  sequence 1..146304022 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ADA18_HUMAN
CC   -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC       spermatogenesis and fertilization. This is a non catalytic
CC       metalloprotease-like protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y3Q7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y3Q7-2; Sequence=VSP_012033;
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- DOMAIN: A tripeptide motif (ECD) within disintegrin-like domain
CC       could be involved in the binding to egg integrin receptor and thus
CC       could mediate sperm/egg binding (By similarity).
CC   -!- PTM: The prodomain and the metalloprotease-like domain are cleaved
CC       during the epididymal maturation of the spermatozoa (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC   -!- GENE_FAMILY: HOG000230883 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000168619;ENST00000265707;ENSP00000265707.
DR   EMBL; AJ133004; - ;
DR   EMBL; AK313961; - ;
DR   EMBL; AY358321; - ;
DR   EMBL; BC121045; - ;
DR   EMBL; BC121046; - ;
DR   UniProtKB/Swiss-Prot; Q9Y3Q7; B2R9Y0; Q0VAI4; Q6UXJ9; -.
DR   EMBL; AJ133004; CAB40812.1; -; mRNA.
DR   EMBL; AY358321; AAQ88687.1; -; mRNA.
DR   EMBL; AK313961; BAG36677.1; -; mRNA.
DR   EMBL; BC121045; AAI21046.1; -; mRNA.
DR   IPI; IPI00003365; -.
DR   IPI; IPI00479446; -.
DR   RefSeq; NP_055052.1; NM_014237.2.
DR   UniGene; Hs.127930; -.
DR   ProteinModelPortal; Q9Y3Q7; -.
DR   SMR; Q9Y3Q7; 179-661.
DR   STRING; Q9Y3Q7; -.
DR   MEROPS; M12.957; -.
DR   PhosphoSite; Q9Y3Q7; -.
DR   PRIDE; Q9Y3Q7; -.
DR   Ensembl; ENST00000265707; ENSP00000265707; ENSG00000168619.
DR   GeneID; 8749; -.
DR   KEGG; hsa:8749; -.
DR   UCSC; uc003xni.1; human.
DR   UCSC; uc010lwx.1; human.
DR   CTD; 8749; -.
DR   GeneCards; GC08P037975; -.
DR   H-InvDB; HIX0034291; -.
DR   HGNC; HGNC:196; ADAM18.
DR   HPA; HPA027605; -.
DR   neXtProt; NX_Q9Y3Q7; -.
DR   PharmGKB; PA24513; -.
DR   eggNOG; prNOG13297; -.
DR   GeneTree; ENSGT00590000082741; -.
DR   InParanoid; Q9Y3Q7; -.
DR   OMA; GTAYCYN; -.
DR   OrthoDB; EOG4P8FHF; -.
DR   PhylomeDB; Q9Y3Q7; -.
DR   NextBio; 32825; -.
DR   ArrayExpress; Q9Y3Q7; -.
DR   Bgee; Q9Y3Q7; -.
DR   CleanEx; HS_ADAM18; -.
DR   Genevestigator; Q9Y3Q7; -.
DR   GermOnline; ENSG00000168619; Homo sapiens.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; TAS:ProtInc.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Gene3D; G3DSA:3.40.390.10; G3DSA:3.40.390.10; 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   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   HOGENOMDNA; HS8.PE1198; -.
KW   ENSG000001686191755old_1320000031; ENSP000002657077901old_1320000031;
KW   Q0VAI3_HUMAN; AJ133004; AK313961; AY358321; BC121045; BC121046;
KW   Alternative splicing; Complete proteome; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Polymorphism; Reference proteome; Signal; Spermatogenesis;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   739 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MFLLLALLTE LGRLQAHEGS EGIFLHVTVP RKIKSNDSEV SERKMIYIIT IDGQPYTLHL
     GKQSFLPQNF LVYTYNETGS LHSVSPYFMM HCHYQGYAAE FPNSFVTLSI CSGLRGFLQF
     ENISYGIEPV ESSARFEHII YQMKNNDPNV SILAVNYSHI WQKDQPYKVP LNSQIKNLSK
     LLPQYLEIYI IVEKALYDYM GSEMMAVTQK IVQVIGLVNT MFTQFKLTVI LSSLELWSNE
     NQISTSGDAD DILQRFLAWK RDYLILRPHD IAYLLVYRKH PKYVGATFPG TVCNKSYDAG
     IAMYPDAIGL EGFSVIIAQL LGLNVGLTYD DITQCFCLRA TCIMNHEAVS ASGRKIFSNC
     SMHDYRYFVS KFETKCLQKL SNLQPLHQNQ PVCGNGILES NEECDCGNKN ECQFKKCCDY
     NTCKLKGSVK CGSGPCCTSK CELSIAGTPC RKSIDPECDF TEYCNGTSSN CVPDTYALNG
     RLCKLGTAYC YNGQCQTTDN QCAKIFGKGA QGAPFACFKE VNSLHERSEN CGFKNSQPLP
     CERKDVLCGK LACVQPHKNA NKSDAQSTVY SYIQDHVCVS IATGSSMRSD GTDNAYVADG
     TMCGPEMYCV NKTCRKVHLM GYNCNATTKC KGKGICNNFG NCQCFPGHRP PDCKFQFGSP
     GGSIDDGNFQ KSGDFYTEKG YNTHWNNWFI LSFCIFLPFF IVFTTVIFKR NEISKSCNRE
     NAEYNRNSSV VSESDDVGH
//

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