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PAG4_SHEEP
ID   PAG4_SHEEP              Reviewed;         380 AA.
AC   P83495; O02724;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Pregnancy-associated glycoprotein 4;
DE            Short=ovPAG4;
DE            EC=3.4.23.-;
DE   AltName: Full=Pregnancy-associated glycoprotein 58c;
DE            Short=ovPAG 58c;
DE   Flags: Precursor;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Placenta;
RX   PubMed=9408244; DOI=10.1095/biolreprod57.6.1384;
RA   Xie S., Green J., Bao B., Beckers J.F., Valdez K.E., Hakami L.,
RA   Roberts R.M.;
RT   "Multiple pregnancy-associated glycoproteins are secreted by day 100 ovine
RT   placental tissue.";
RL   Biol. Reprod. 57:1384-1393(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=9371757; DOI=10.1073/pnas.94.24.12809;
RA   Xie S., Green J., Bixby J.B., Szafranska B., DeMartini J.C., Hecht S.,
RA   Roberts R.M.;
RT   "The diversity and evolutionary relationships of the pregnancy-associated
RT   glycoproteins, an aspartic proteinase subfamily consisting of many
RT   trophoblast-expressed genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12809-12816(1997).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 54-76, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Fetal cotyledon {ECO:0000269|PubMed:15460157};
RX   PubMed=15460157; DOI=10.1051/rnd:2004025;
RA   El Amiri B., Remy B., De Sousa N.M., Beckers J.F.;
RT   "Isolation and characterization of eight pregnancy-associated glycoproteins
RT   present at high levels in the ovine placenta between day 60 and day 100 of
RT   gestation.";
RL   Reprod. Nutr. Dev. 44:169-181(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10819764; DOI=10.1095/biolreprod62.6.1624;
RA   Green J.A., Xie S., Quan X., Bao B., Gan X., Mathialagan N., Beckers J.F.,
RA   Roberts R.M.;
RT   "Pregnancy-associated bovine and ovine glycoproteins exhibit spatially and
RT   temporally distinct expression patterns during pregnancy.";
RL   Biol. Reprod. 62:1624-1631(2000).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:9408244}.
CC   -!- TISSUE SPECIFICITY: Trophoblast and placental tissue. Produced
CC       specifically in the invasive binucleate cells of the placenta.
CC       {ECO:0000269|PubMed:10819764, ECO:0000269|PubMed:15460157,
CC       ECO:0000269|PubMed:9371757, ECO:0000269|PubMed:9408244}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the later stages of pregnancy between
CC       day 60 and day 100 of gestation. {ECO:0000269|PubMed:10819764,
CC       ECO:0000269|PubMed:15460157, ECO:0000269|PubMed:9408244}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; U94790; AAB53225.1; -; mRNA.
DR   RefSeq; NP_001009462.1; NM_001009462.1.
DR   AlphaFoldDB; P83495; -.
DR   SMR; P83495; -.
DR   MEROPS; A01.089; -.
DR   GeneID; 443536; -.
DR   CTD; 337898; -.
DR   OrthoDB; 1619495at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; PTHR47966; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..53
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:15460157"
FT                   /id="PRO_0000425540"
FT   CHAIN           54..380
FT                   /note="Pregnancy-associated glycoprotein 4"
FT                   /id="PRO_0000199523"
FT   DOMAIN          71..377
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        102..107
FT                   /evidence="ECO:0000250"
FT   DISULFID        261..265
FT                   /evidence="ECO:0000250"
FT   DISULFID        303..337
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  42762 MW;  D58242542B624283 CRC64;
     MKWLVLLGLV AFSECIFKIP LRRVKTMRKT LSGKNMLNDV LKEHPYRLPQ ISFRGSNLII
     HPLRNIRDTF YVGNITIGTP PQEFQVLFDT GSSVLWVPSV LCNSSTCSIH VRFRHLQSST
     FRTTNKTFWI TYGAGTMKGV VAHDTVRIGD LVSIDQPFGL SMAEYGFHGR RFDGVLGLNY
     PRQSCCRPTP IFDKLKNQGA ISEPVFAFYL SKDEQEGSVV MFGGVDHRYY KGELNWVPLV
     KADDWTIQVD RISMRREVIA CSDGCDALLD TGASFIHGPG RLIDDIQKLI GSEPRDLKHY
     ISCSAVNTLP SIIFTINGIN YPVPAQAYIL KGSTGHCYTA FRAKRVRTST ESWVLGDVFL
     RLYFSVFDRG NDRIGLAPAM
 
 
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