SPAD1_BOVIN
ID SPAD1_BOVIN Reviewed; 134 AA.
AC P29392; Q2YDJ6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Spermadhesin-1;
DE AltName: Full=Acidic seminal fluid protein;
DE Short=ASFP;
DE Flags: Precursor;
GN Name=SPADH1;
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 TISSUE=Seminal vesicle;
RX PubMed=1543494; DOI=10.1016/0006-291x(92)91633-2;
RA Wempe F., Einspanier R., Scheit K.H.;
RT "Characterization by cDNA cloning of the mRNA of a new growth factor from
RT bovine seminal plasma: acidic seminal fluid protein.";
RL Biochem. Biophys. Res. Commun. 183:232-237(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 21-43.
RC TISSUE=Seminal vesicle;
RX PubMed=1898381; DOI=10.1016/0006-291x(91)91918-3;
RA Einspanier R., Einspanier A., Wempe F., Scheit K.H.;
RT "Characterization of a new bioactive protein from bovine seminal fluid.";
RL Biochem. Biophys. Res. Commun. 179:1006-1010(1991).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=8181566; DOI=10.1016/0014-5793(94)00362-9;
RA Einspanier R., Krause I., Calvete J.J., Toepfer-Petersen E.,
RA Klostermeyer H., Karg H.;
RT "Bovine seminal plasma aSFP: localization of disulfide bridges and
RT detection of three different isoelectric forms.";
RL FEBS Lett. 344:61-64(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9334740; DOI=10.1038/nsb1097-783;
RA Romero A., Romao M.J., Varela P.F., Koelln I., Dias J.M., Carvalho A.L.,
RA Sanz L., Toepfer-Petersen E., Calvete J.J.;
RT "The crystal structures of two spermadhesins reveal the CUB domain fold.";
RL Nat. Struct. Biol. 4:783-788(1997).
CC -!- FUNCTION: Stimulates cell division and progesterone secretion of bovine
CC granulosa cells in vitro in a potent and dose dependent manner. This
CC protein appears to be a potent growth factor with effects on ovarian
CC granulosa cells.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seminal vesicle tissue, ampulla and weakly in
CC tissue of epididymis.
CC -!- SIMILARITY: Belongs to the spermadhesin family. {ECO:0000305}.
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DR EMBL; M84603; AAA30745.1; -; mRNA.
DR EMBL; BC110191; AAI10192.1; -; mRNA.
DR PIR; JQ1403; JQ1403.
DR RefSeq; NP_777041.1; NM_174616.3.
DR PDB; 1SFP; X-ray; 1.90 A; A=21-134.
DR PDBsum; 1SFP; -.
DR AlphaFoldDB; P29392; -.
DR SMR; P29392; -.
DR STRING; 9913.ENSBTAP00000014297; -.
DR PaxDb; P29392; -.
DR PRIDE; P29392; -.
DR Ensembl; ENSBTAT00000014297; ENSBTAP00000014297; ENSBTAG00000010796.
DR GeneID; 282373; -.
DR KEGG; bta:282373; -.
DR CTD; 282373; -.
DR VEuPathDB; HostDB:ENSBTAG00000010796; -.
DR eggNOG; ENOG502TD48; Eukaryota.
DR GeneTree; ENSGT00390000012112; -.
DR InParanoid; P29392; -.
DR OMA; AFSTFYY; -.
DR OrthoDB; 1512831at2759; -.
DR EvolutionaryTrace; P29392; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000010796; Expressed in mammary gland fat and 32 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000124; Spermadhesin.
DR Pfam; PF00431; CUB; 1.
DR SMART; SM00042; CUB; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00985; SPERMADHESIN_1; 1.
DR PROSITE; PS00986; SPERMADHESIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Growth factor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1898381"
FT CHAIN 21..134
FT /note="Spermadhesin-1"
FT /id="PRO_0000033187"
FT DOMAIN 30..131
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 30..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000269|PubMed:8181566"
FT DISULFID 74..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000269|PubMed:8181566"
FT CONFLICT 43
FT /note="T -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:1SFP"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 90..103
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1SFP"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1SFP"
SQ SEQUENCE 134 AA; 15036 MW; 339BCFF8637D64C0 CRC64;
MKLSSVIPWA LLLSTATVDS MDWLPRNTNC GGILKEESGV IATYYGPKTN CVWTIQMPPE
YHVRVSIQYL QLNCNKESLE IIDGLPGSPV LGKICEGSLM DYRSSGSIMT VKYIREPEHP
ASFYEVLYFQ DPQA
