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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0378-1119(99)00302-9; PubMed=10524237 [NCBI, ExPASy, EBI, Israel, Japan]
Poindexter K.,
Nelson N.,
DuBose R.F.,
Black R.A.,
Cerretti D.P.;
"The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries.";
Gene 237:61-70(1999).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] OF 181-722.
TISSUE=Testis;
DOI=10.1016/S0378-1119(97)00597-0; PubMed=9469942 [NCBI, ExPASy, EBI, Israel, Japan]
Hooft van Huijsduijnen R.;
"ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin-alpha.";
Gene 206:273-282(1998).
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- FUNCTION: May be involved in sperm maturation and/or fertilization. May also be involved in epithelia functions associated with establishing and maintaining gradients of ions or nutrients.
- COFACTOR: Binds 1 zinc ion per subunit (Potential).
- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
- DOMAIN: A tripeptide motif (VGE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding.
- DOMAIN: The cysteine-rich domain encodes putative cell-fusion peptides, which could be involved in sperm-egg fusion.
- DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
- PTM: Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.
- MISCELLANEOUS: May be the functional equivalent of ADAM 1/fertilin alpha which is a pseudogene in human.
- SIMILARITY: Contains 1 disintegrin domain.
- SIMILARITY: Contains 1 EGF-like domain.
- SIMILARITY: Contains 1 peptidase M12B domain [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 722 AA [This is the length of the unprocessed precursor] |
Molecular weight: 80820 Da [This is the MW of the unprocessed precursor] |
CRC64: 25DFD896F8A1876A [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAVDGTLVYI RVTLLLLWLG VFLSISGYCQ AGPSQHFTSP EVVIPLKVIS RGRSAKAPGW
70 80 90 100 110 120
LSYSLRFGGQ KHVVHMRVKK LLVSRHLPVF TYTDERALLE DQLFIPDDCY YHGYVEGAPE
130 140 150 160 170 180
SLVVFSACFG GFRGVLKISG LTYEIEPIRH SATFEHLVYK VNSNETQFPA MRCGLTEKEV
190 200 210 220 230 240
ARQQLEFEEA ENSALEPKSA GDWWTHAWFL ELVVVVNHDF FIYSQSNISK VQEDVFLVVN
250 260 270 280 290 300
IVDSMYQQLG TYIILIGIEI WNQGNVFPMT SIEQVLNDFS QWKQISLSQL QHDAAHMFIK
310 320 330 340 350 360
NSLISILGLA YVAGICRPPI DCGVDNFQGD TWSLFANTVA HELGHTLGMQ HDEEFCFCGE
370 380 390 400 410 420
RGCIMNTFRV PAEKFTNCSY ADFMKTTLNQ GSCLHNPPRL GEIFMLKRCG NGVVEREEQC
430 440 450 460 470 480
DCGSVQQCEQ DACCLLNCTL RPGAACAFGL CCKDCKFMPS GELCRQEVNE CDLPEWCNGT
490 500 510 520 530 540
SHQCPEDRYV QDGIPCSDSA YCYQKRCNNH DQHCREIFGK DAKSASQNCY KEINSQGNRF
550 560 570 580 590 600
GHCGINGTTY LKCHISDVFC GRVQCENVRD IPLLQDHFTL QHTHINGVTC WGIDYHLRMN
610 620 630 640 650 660
ISDIGEVKDG TVCGPGKICI HKKCVSLSVL SHVCLPETCN MKGICNNKHH CHCGYGWSPP
670 680 690 700 710 720
YCQHRGYGGS IDSGPASAKR GVFLPLIVIP SLSVLTFLFT VGLLMYLRQC SGPKETKAHS
SG
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Q9UKJ8 in FASTA format |
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ExPASy Home page
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