BSPH1_MOUSE
ID BSPH1_MOUSE Reviewed; 133 AA.
AC Q3UW26; B2RVZ6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Binder of sperm protein homolog 1;
DE AltName: Full=Bovine seminal plasma protein homolog 1;
DE AltName: Full=Bovine seminal plasma protein-like 1;
DE Flags: Precursor;
GN Name=Bsph1; Synonyms=Gm767;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Epididymis;
RX PubMed=17085770; DOI=10.1093/molehr/gal098;
RA Lefebvre J., Fan J., Chevalier S., Sullivan R., Carmona E., Manjunath P.;
RT "Genomic structure and tissue-specific expression of human and mouse genes
RT encoding homologues of the major bovine seminal plasma proteins.";
RL Mol. Hum. Reprod. 13:45-53(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=22539676; DOI=10.1095/biolreprod.111.096644;
RA Plante G., Therien I., Manjunath P.;
RT "Characterization of recombinant murine binder of sperm protein homolog 1
RT and its role in capacitation.";
RL Biol. Reprod. 87:1-11(2012).
RN [5]
RP FUNCTION.
RX PubMed=24307707; DOI=10.1095/biolreprod.113.114272;
RA Plante G., Fan J., Manjunath P.;
RT "Murine Binder of SPerm homolog 2 (BSPH2): the black sheep of the BSP
RT superfamily.";
RL Biol. Reprod. 90:20-20(2014).
RN [6]
RP FUNCTION.
RX PubMed=25602034; DOI=10.1530/rep-14-0559;
RA Plante G., Manjunath P.;
RT "Murine binder of sperm protein homolog 1: a new player in HDL-induced
RT capacitation.";
RL Reproduction 149:367-376(2015).
CC -!- FUNCTION: Binds sperm in vitro and promotes sperm capacitation
CC (PubMed:22539676, PubMed:24307707). Specifically promotes capacitation
CC induced by high density lipoproteins (HDLs) (PubMed:25602034). Also
CC binds heparin, phospholipid liposomes, and weakly to gelatin
CC (PubMed:22539676). Does not bind chondroitin sulfate B
CC (PubMed:22539676). {ECO:0000269|PubMed:22539676,
CC ECO:0000269|PubMed:24307707, ECO:0000269|PubMed:25602034}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed only in the epididymis.
CC {ECO:0000269|PubMed:17085770}.
CC -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC {ECO:0000305}.
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DR EMBL; DQ227498; ABB71592.1; -; mRNA.
DR EMBL; AK136662; BAE23093.1; -; mRNA.
DR EMBL; BC147454; AAI47455.1; -; mRNA.
DR EMBL; BC147459; AAI47460.1; -; mRNA.
DR CCDS; CCDS20832.1; -.
DR RefSeq; NP_001028590.1; NM_001033418.4.
DR RefSeq; NP_001288611.1; NM_001301682.1.
DR AlphaFoldDB; Q3UW26; -.
DR SMR; Q3UW26; -.
DR STRING; 10090.ENSMUSP00000096408; -.
DR GlyGen; Q3UW26; 1 site.
DR PhosphoSitePlus; Q3UW26; -.
DR PaxDb; Q3UW26; -.
DR PRIDE; Q3UW26; -.
DR ProteomicsDB; 265246; -.
DR Antibodypedia; 70932; 4 antibodies from 4 providers.
DR Ensembl; ENSMUST00000098811; ENSMUSP00000096408; ENSMUSG00000074378.
DR GeneID; 330470; -.
DR KEGG; mmu:330470; -.
DR UCSC; uc009ffw.2; mouse.
DR CTD; 100131137; -.
DR MGI; MGI:2685613; Bsph1.
DR VEuPathDB; HostDB:ENSMUSG00000074378; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000163003; -.
DR HOGENOM; CLU_126630_1_0_1; -.
DR InParanoid; Q3UW26; -.
DR OMA; CIKSKSR; -.
DR OrthoDB; 1429125at2759; -.
DR PhylomeDB; Q3UW26; -.
DR TreeFam; TF343543; -.
DR BioGRID-ORCS; 330470; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q3UW26; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UW26; protein.
DR Bgee; ENSMUSG00000074378; Expressed in striatum and 3 other tissues.
DR ExpressionAtlas; Q3UW26; baseline and differential.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0048240; P:sperm capacitation; IDA:MGI.
DR CDD; cd00062; FN2; 1.
DR Gene3D; 2.10.10.10; -; 2.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR016356; Seminal_plasma_PDC-109-like.
DR Pfam; PF00040; fn2; 2.
DR PIRSF; PIRSF002541; Seminal_plasma_PDC-109; 1.
DR SMART; SM00059; FN2; 2.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Fertilization; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..133
FT /note="Binder of sperm protein homolog 1"
FT /id="PRO_0000326157"
FT DOMAIN 40..84
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 85..133
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 59..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 90..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 104..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 133 AA; 16014 MW; 0C1BCD47FDC66F86 CRC64;
MAQPLDFLLV SICLFHSLFS FQVEDYYAPT IESLIRNPET EDGACVFPFL YRSEIFYDCV
NFNLKHKWCS LNKTYQGYWK YCALSDYAPC AFPFWYRHMI YWDCTEDGEV FGKKWCSLTP
NYNKDQVWKY CIE
