TKDP1_SHEEP
ID TKDP1_SHEEP Reviewed; 265 AA.
AC Q29428;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Trophoblast Kunitz domain protein 1;
DE Short=TKDP-1;
DE Flags: Precursor;
GN Name=TKDP1;
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.
RC TISSUE=Conceptus membrane, and Uterus;
RX PubMed=7510284; DOI=10.1016/s0021-9258(17)37276-9;
RA Kramer K.K., Duffy J.Y., Klemann S.W., Bixby J.A., Low B.G., Pope W.F.,
RA Roberts R.M.;
RT "Selective cloning of cDNA for secretory proteins of early embryos.
RT Identification of a transiently expressed Kunitz domain protein from
RT preimplantation sheep trophoblast.";
RL J. Biol. Chem. 269:7255-7261(1994).
CC -!- FUNCTION: May play a role in mediating maternal-conceptus interactions
CC in the immediate preimplantation period. Does not seem to have
CC proteinase inhibitory activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed only in the trophectoderm, which forms
CC the outer epithelial layer of the trophoblast.
CC -!- DEVELOPMENTAL STAGE: Maximal expression at days 14 and 16 of pregnancy.
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DR EMBL; U00165; AAA19108.1; -; Unassigned_DNA.
DR EMBL; L11343; AAB46361.1; -; mRNA.
DR PIR; A53390; A53390.
DR RefSeq; NP_001009291.1; NM_001009291.1.
DR AlphaFoldDB; Q29428; -.
DR SMR; Q29428; -.
DR Ensembl; ENSOART00020021751; ENSOARP00020018004; ENSOARG00020014222.
DR GeneID; 443303; -.
DR KEGG; oas:443303; -.
DR CTD; 404076; -.
DR OrthoDB; 483422at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..265
FT /note="Trophoblast Kunitz domain protein 1"
FT /id="PRO_0000016880"
FT REPEAT 32..115
FT /note="1"
FT REPEAT 117..200
FT /note="2"
FT DOMAIN 208..258
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 32..200
FT /note="2 X 84 AA approximate repeats"
FT SITE 218..219
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 208..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 217..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 233..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 265 AA; 28964 MW; D700805DF03E3132 CRC64;
MRQLCLSTAL LFLLVILVDS TPLNIYHIQD EGLETSHRRG PEKRSVIDVV SGIINGVATG
TKIIEKGAGI LTGLAEIITK AIKGQVMISR IQFDNHTLEE LPTLQLEYST LSEENNGLKT
SHRRGLEKRS VTDVVTSIIN GVATGTKIIE KGAGILTGLA EIITKAIKGQ VMISGIQFDN
HTLEEYQTLK IEYSTLSEEN KASKPALCLE PKVTGDCNAT MTRYFYNTQT GLCEQFVYTG
CEGNGNNFEN LEDCMKTCSQ EAGSL
