ID   UFAP_PIG                Reviewed;         417 AA.
AC   P16708;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Uteroferrin-associated protein;
DE            Short=UFAP;
DE   Flags: Precursor;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 41-60 AND 100-119.
RC   TISSUE=Uterus;
RX   PubMed=2342477; DOI=10.1210/mend-4-3-428;
RA   Malathy P.-V., Imakawa K., Simmen R.C.M., Roberts R.M.;
RT   "Molecular cloning of the uteroferrin-associated protein, a major
RT   progesterone-induced serpin secreted by the porcine uterus, and the
RT   expression of its mRNA during pregnancy.";
RL   Mol. Endocrinol. 4:428-440(1990).
CC   -!- SUBUNIT: Heterodimer with the iron-binding acid phosphatase, UF.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- DEVELOPMENTAL STAGE: Levels in the endometrium increase as pregnancy
CC       proceeds, reaching maximal levels around day 70 and then remain
CC       relatively constant in late gestation (days 70-110).
CC   -!- INDUCTION: By progesterone.
CC   -!- PTM: A series of at least four post-translational proteolytic
CC       processing steps and differential N-linked glycosylation generate
CC       various molecular forms. Three mature forms starting at positions 41,
CC       45 and 100 are produced.
CC   -!- PTM: Glycosylated; contains the so-called mannose 6-phosphate lysosomal
CC       recognition marker.
CC   -!- MISCELLANEOUS: The UFAP are a group of three (MW 42 kDa, 48 kDa, and 50
CC       kDa) antigenically related, basic glycoproteins secreted by the porcine
CC       uterus.
CC   -!- SIMILARITY: Belongs to the serpin family. UTMP subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M30315; AAA31137.1; -; mRNA.
DR   PIR; A34722; A34722.
DR   AlphaFoldDB; P16708; -.
DR   SMR; P16708; -.
DR   MEROPS; I04.981; -.
DR   PRIDE; P16708; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Pregnancy; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..40
FT                   /note="Or 44, or 99"
FT                   /evidence="ECO:0000269|PubMed:2342477"
FT                   /id="PRO_0000032533"
FT   CHAIN           41..417
FT                   /note="Uteroferrin-associated protein"
FT                   /id="PRO_0000032534"
FT   SITE            378..379
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  47760 MW;  9AA6883B221781F5 CRC64;
     MSHGKMPLVL SLVLILCGLF NSISCEKQQT SPKTITPVSF KRIAALSQKM EANYKAFAQE
     LFKTLLIEDP RKNMIFSPVS ISISLATLSL GLRSATRTNA IDVLDVALKN LAVMLMAQAP
     TALLEIVHEL VNRTAKHQDI LIDRTEMNQM FLKEIDRYIK MDIQMIDFKD KEKTKKAINQ
     FVADKIDKKA KNLITHLDPQ TLLCLVNYIF FKGILERAFQ TNLTKKEDFF VNEKTIVQVD
     MMRKTERMIY SRSEELLATM VKIPCKENAS IILVLPDTGK FNFALKEMAA KRARLQKTND
     FRLVHLVVPK IKDNLQDRFK HLLPKIGIND IFTTKAVTWN TTGTSTILEA VHHAVIEVKE
     DGLTKNAAKD KDFWKVPVDK KEVPVVVKFD RPFFLFVEDE ITRRDLFVAK VFNPKTE