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- FUNCTION: Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity).
- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
- CATALYTIC ACTIVITY: A dinucleotide + H2O = 2 mononucleotides.
- COFACTOR: Binds 2 divalent metal cations per subunit (Probable).
- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated active site intermediate is formed which inhibits further ATP hydrolysis.
- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein (Potential). Secreted (By similarity). Note=Located to the apical surface in intestinal and kidney epithelial cells. Located to the cell surface of basophils, and to the apical plasma membrane of bile duct cells. Secreted in serum, and in lumen of epithelial cells (By similarity).
- PTM: N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal (By similarity).
- PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.
- SIMILARITY: Contains 2 SMB (somatomedin-B) domains.
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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: 874 AA [This is the length of the unprocessed precursor] |
Molecular weight: 99523 Da [This is the MW of the unprocessed precursor] |
CRC64: A901CC5B7E787F40 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MQSTLNLSTE EPVKRNTVKK YKIICIVLLI LLVAVSLALG LVAGLRQQEE QGSCRKKCFD
70 80 90 100 110 120
ASHRGLEGCR CDVGCKGRGD CCWDFEDTCV QSTQIWTCNK FRCGETRLES SLCSCSDDCL
130 140 150 160 170 180
QRKDCCADYK SVCQGETSWV DEDCSTAQQP QCPEGFDLPP VILFSMDGFR AEYLQTWSTL
190 200 210 220 230 240
VPNINKLKTC GVHSQYLRPA YPTKTFPNHY TIVTGLYPES HGIIDNNMYD INLNKNFSLS
250 260 270 280 290 300
SKEKDNPAWW QGQPIWLTAM YQGLKVGTYF WPGSDVAING TFPSIYKIYN RSVTYEERIF
310 320 330 340 350 360
TLLKWLDLPK AERPDFYTIY VEEPDSQGHN YGPVSAGVIQ ALQLVDKTFG LLMEGLKQRN
370 380 390 400 410 420
LVNCVNIILL ADHGMDQTYC DKLEYMADYF SSINFYMFEG PAPRIRTRNI PQDFFTFNSE
430 440 450 460 470 480
EIVRNLSCRK PDQHFKPYLS PDLPKRLHFA KNVRIDKVNL LVDRQWQAVR NRAYSYCGGG
490 500 510 520 530 540
NHGYDNEFKS MEAIFLAHGP SFKQKTEVEP FDNIEVYNLL CDLLHIQPAP NNGTHGSLNH
550 560 570 580 590 600
LLKVPFYEPS HAEELSKFSV CGFTVPLPTD TLGCSCSRLQ TNSDLERVNQ MLDLTQDEIT
610 620 630 640 650 660
ATEKLNLPFG RPRLIQKNKE PCLLYHREYV SGFDKTLRMP LWSSYTVPKP GDTSPLPPTV
670 680 690 700 710 720
PDCLRADVRV APSESQNCSF SLADKNITHG FLYPPANNRT SNSQYDALIT SNLVPMYEAF
730 740 750 760 770 780
KTMWNYFHSV LLVKYAMERN GVNVVSGPVF DYDYDGHFDA PDEIADYAVN TSVPIPTHYF
790 800 810 820 830 840
VVLTSCKNQS QTPDACTGWL DVLPFVIPHR PTNVESCPEN KSESLWVEER FNVHTARVRD
850 860 870
VELLTGLDFY QEKAQPVSEI LQLKTYLPVF ETVI
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P15396 in FASTA format |
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