TKDP1_BOVIN
ID TKDP1_BOVIN Reviewed; 351 AA.
AC Q28201; Q9N0X8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Trophoblast Kunitz domain protein 1;
DE Short=TKDP-1;
DE Flags: Precursor;
GN Name=TKDP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hereford X Simmental;
RA Green J.A., Maclean J.A. II, Gan X., Xie S., Roberts R.M.;
RT "Cloning and characterization of the expression of trophoblast Kunitz
RT domain proteins (TKDP).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-351.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Maximal expression at days 17-19 of pregnancy.
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DR EMBL; AF241776; AAF61247.1; -; mRNA.
DR EMBL; L11344; AAA30795.1; -; mRNA.
DR RefSeq; NP_991345.1; NM_205776.1.
DR AlphaFoldDB; Q28201; -.
DR SMR; Q28201; -.
DR STRING; 9913.ENSBTAP00000052527; -.
DR GeneID; 404076; -.
DR KEGG; bta:404076; -.
DR CTD; 404076; -.
DR eggNOG; KOG4597; Eukaryota.
DR OrthoDB; 483422at2759; -.
DR Proteomes; UP000009136; 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 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..351
FT /note="Trophoblast Kunitz domain protein 1"
FT /id="PRO_0000016879"
FT REPEAT 32..116
FT /note="1"
FT REPEAT 117..201
FT /note="2"
FT REPEAT 202..286
FT /note="3"
FT DOMAIN 294..344
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT REGION 32..286
FT /note="3 X 84 AA approximate tandem repeats"
FT SITE 304..305
FT /note="Reactive bond homolog"
FT /evidence="ECO:0000250"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 294..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 303..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 319..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT CONFLICT 274
FT /note="L -> P (in Ref. 2; AAA30795)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="N -> T (in Ref. 2; AAA30795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38255 MW; 13DBAF9AA25FEB35 CRC64;
MRQLCLSSAL LFLLVILVDS TPLNIHHIQD EGVETSHRRG PEKRSVIDVV TSIIDGVATG
TKIVKNGAGL LTGLAEIITK AIKGQVMISR IQFDNHTQEE LPTLNIEYST LSEENKGVET
SHRKGPEKRS VIDVVTSIID GVATGTKIVT KGASILTGLA EIINKAIRGQ VMISRIQFNN
HTLEEFPKLN IEYSTLSEDN TGVETSRRRG PEKRSVIDVV TSIIDGVATG TKIVKKGTSI
LTGLAEIINK AIKGQVMISG IQFNNHTLEE YQTLKIEYSA LNEENKAASK PALCLEPKVT
GGCNAVMTRY FYNAQNGLCE QFVYDGCEGN GNNFEKLEDC MKTCSQEAGS L