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Database: UniProt
Entry: H0VSW2_CAVPO
LinkDB: H0VSW2_CAVPO
Original site: H0VSW2_CAVPO 
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
//
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