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[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS.
STRAIN=Lewis, Louvain, and Wistar;
DOI=10.1046/j.1365-2370.2002.00330.x; PubMed=12121276 [NCBI, ExPASy, EBI, Israel, Japan]
Banakh I.,
Sali A.,
Dubljevic V.,
Grobben B.,
Slegers H.,
Goding J.W.;
"Structural basis of allotypes of ecto-nucleotide pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein PC-1) in the mouse and rat, and analysis of allele-specific xenogeneic antibodies.";
Eur. J. Immunogenet. 29:307-313(2002).
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- FUNCTION: Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity (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 intermediate is formed which inhibits further hydrolysis.
- SUBUNIT: Homodimer; disulfide-linked (By similarity).
- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. Note=Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side (By similarity).
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | 1 |
| Isoform ID | Q924C3-2 |
| Features which should be applied to build the isoform sequence: VSP_006749. |
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- DOMAIN: The di-leucine motif is required for basolateral targeting in epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells (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.
- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
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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: 906 AA [This is the length of the unprocessed precursor] |
Molecular weight: 102942 Da [This is the MW of the unprocessed precursor] |
CRC64: 71F56780B279A919 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART AKDPNTYKVL
70 80 90 100 110 120
SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS NCRCDAACVS LGNCCLDFQE
130 140 150 160 170 180
TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD DCKAHNDCCI NYSSVCQEKK SWVEEACETI
190 200 210 220 230 240
DAPQCPAEFE SPPTLLFSLD GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP
250 260 270 280 290 300
NHYSIVTGLY PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG
310 320 330 340 350 360
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY TLYLEEPDSS
370 380 390 400 410 420
GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL ILISDHGMEQ GSCKKYVYLN
430 440 450 460 470 480
KYLGDVNNVK VVYGPAARLR PTEVPETYYS FNYEALAKNL SCRETNQHFR PYLKHFLPKR
490 500 510 520 530 540
LHFAKNDRIE PLTFYLDPQW QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG
550 560 570 580 590 600
AEVDSFENIE VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS
610 620 630 640 650 660
VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH RVCLLHQQQF
670 680 690 700 710 720
LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP LSPMHKCSYY KSTSKLSYGF
730 740 750 760 770 780
LTPPRLNRVS RQIYSEALLT SNIVPMYQSF QVIWQYLHDT VLRRYAQERN GVNVVSGPVF
790 800 810 820 830 840
DFDYDGRYDS SEILKQNTRV IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP
850 860 870 880 890 900
HRPDNIESCT HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP
IFSQED
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Q924C3 in FASTA format |
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