ID H0VSW2_CAVPO Unreviewed; 823 AA.
AC H0VSW2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase 2 {ECO:0000313|Ensembl:ENSCPOP00000013731.3};
GN Name=ENPP2 {ECO:0000313|Ensembl:ENSCPOP00000013731.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000013731.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000013731.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013731.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00010594}.
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DR EMBL; AAKN02000096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02000097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02000098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0VSW2; -.
DR Ensembl; ENSCPOT00000015381.3; ENSCPOP00000013731.3; ENSCPOG00000015234.4.
DR VEuPathDB; HostDB:ENSCPOG00000015234; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000155778; -.
DR HOGENOM; CLU_012256_0_0_1; -.
DR TreeFam; TF330032; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000015234; Expressed in uterine cervix and 13 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR CDD; cd16018; Enpp; 1.
DR Gene3D; 4.10.410.20; -; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF21; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE FAMILY MEMBER 2; 1.
DR Pfam; PF01663; Phosphodiest; 2.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF90188; Somatomedin B domain; 2.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..823
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012768166"
FT DOMAIN 55..98
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 99..143
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
SQ SEQUENCE 823 AA; 94001 MW; 6E09450E8786152F CRC64;
MAAGGSARPG QVLSLFTLAI GVHICLGATV SRVKRAEGWE ESLPSVLSDS PWTNTSGSCK
GRCFELQEVG PPDCRCDNLC KSYSSCCHDF DQLCLKTARG WECTKDRCGE ARDEEHACHC
SEDCLARGDC CTNYHVVCKG ESHWVDDDCE EIKAPECPAG FVRPPLIIFS VDGFRASYMK
KSTKLMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
TFHLRGREKF NHRWWGGQPV THTNEIRGWF VPNSSIPHER RILTILQWLS LPDHERPSVY
AFYSEQPDFS GHKYGPFGPE MTNPLRDIDR TMGQLMDGLK QLKLHRCVNV IFVGDHGMED
VTCERTEFLS NYLTNVDDIT LVPGTLGRIR PKSNTNAKYD PKVIVANLTC KRPDQHFKPY
LKQHLPKRLH YANNRRIEDV HLLVDRRWHV ASRKPMDSSK KPTGKCFYQG DHGFDNKVSS
MQTVFVGYGP SFKYKTKVPP FENIELYNVM CDLLGLKPAP NNGTHGSLNH LLRSSTFRPV
MPEEVSRPNY PGVMYLQSDF DLGCTCDDKV EPENKLDELN KRLHTKESTE GKELQQKGNM
IGHFEPRKER HLLYGRPAVL YRTRYDILYH TDFESGYSEV FLMPLWTSYT VAKQVAQEVG
FYAFCSIAVL RVWNYFQRVL VKKYASERNG VNVISGPIFD YDYDGLHDTE DKIKQYVEGS
AIPVPTHYYS ILTSCLDFTQ QADKCDGPLS VSAFVLPHRA DNDESCSSSE DESKWVEELI
KMHTARVRDI EQLTSLDFFR KTSRSYPEIL SLKTYLHTYE SEI
//