(data stored in ACNUC30567 zone)

HOGENOM: CAVPO1_65_PE3

ID   CAVPO1_65_PE3                        STANDARD;      PRT;   735 AA.
AC   CAVPO1_65_PE3; Q60411;
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   2; Short=ADAM 2;AltName: Full=Fertilin subunit beta;AltName: Full=PH-30;
DE   Short=PH30;AltName: Full=PH30-beta;Flags: Precursor; (CAVPO1_65.PE3).
GN   Name=ADAM2; Synonyms=FTNB;
OS   CAVIA PORCELLUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAVPO1_65.PE3.
CC       Cavia porcellus scaffold scaffold_1 cavPor3 partial sequence
CC       63229963..64229962 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:ADAM2_CAVPO
CC   -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC       sperm-egg plasma membrane adhesion and fusion during
CC       fertilization. Could have a direct role in sperm-zona binding or
CC       migration of sperm from the uterus into the oviduct. Interactions
CC       with egg membrane could be mediated via binding between its
CC       disintegrin-like domain to one or more integrins receptors on the
CC       egg. This is a non catalytic metalloprotease-like protein (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer with ADAM1/fertilin subunit alpha.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- DEVELOPMENTAL STAGE: Expression begins during meiotic prophase.
CC   -!- DOMAIN: A tripeptide motif (TDE) 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 signal and the metalloprotease domain are cleaved during
CC       the epididymal maturation of the spermatozoa (By 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:Cavia_porcellus;ENSCPOG00000022133;ENSCPOT00000019435;ENSCPOP00000018574.
DR   EMBL; Z11720; - ;
DR   UniProtKB/Swiss-Prot; Q60411; -.
DR   EMBL; Z11720; CAA77784.1; -; mRNA.
DR   PIR; S23403; S23403.
DR   RefSeq; NP_001166381.1; NM_001172910.1.
DR   ProteinModelPortal; Q60411; -.
DR   MEROPS; M12.950; -.
DR   Ensembl; ENSCPOT00000019435; ENSCPOP00000018574; ENSCPOG00000022133.
DR   GeneID; 100135471; -.
DR   CTD; 2515; -.
DR   eggNOG; roNOG10629; -.
DR   GeneTree; ENSGT00590000082741; -.
DR   OrthoDB; EOG49CQ78; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000742; EGF_3.
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   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SMART; SM00181; EGF; 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; 1.
DR   HOGENOMDNA; CAVPO1_65.PE3; -.
KW   ENSCPOG00000022133fold_1320000031; ENSCPOP00000018574fold_1320000031;
KW   Z11720;
KW   Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   735 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLCLLLLLCG LASLGGPLKK YVENSGMQIT VPEKIRSVKR GSVESEVSYK IVIENTTYIV
     NLVRKMFLPH DFQVYSYDSA GIMKPFEDYS QNFCYYQGHI EGFPTSLASI STCAGLRGLL
     QFETVSYGIE PLKSSIGFEH VIYPVKHDNE KSQYLKKSIN VKNVVYKIKS IKSSVRTHYI
     EMHIIVEKNL YKHMGGNTAT VTEKIFQLVG LMNAFFSTLN LTVILASLEL WIDENKIPTT
     GDVNELLHAF QKWKKSYLVL RPHDVHFYSG YRESPSYIGA IFQGMICNTS YGGGIALHSK
     TITLDSFGVI LVQLLSVSMG IAYDNADLCR CRGAICLMSP EAVFSSGMKM FSNCSVKAFK
     LFTSSQVSQC LQNQPYLEPV YRSNPVCGNN RVEQGEDCDC GSQEECQDTC CDAATCRLKS
     TSRCAQGPCC NQCEFKTKGE VCRESTDECD LPEYCNGSSG ACQEDLYVIN GHRCANEEWI
     CMNGRCLSGK AQCQETFGTE MEMGSVDCFE QLNTKNDITG NCGILSPGNY KACGASNWKC
     GKLICSYDKS EILRNKEGMT IYANISGHIC VSIEYPPGHA KSALMWVRDG TVCGPSEVCR
     QQQCVSSSYL GYDCTPATCS DHGVCNNKRH CHCNPTYVPP NCETQDSTKP GGSVDSGNLR
     YEPIPETYFV EGAYHTKSRK WPFFLIIPFF VIFSVLVATV VKVYYQKKKW KTEDYANDEN
     IESESEPKSS KVSSK
//

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