ESPB1_HUMAN
ID ESPB1_HUMAN Reviewed; 223 AA.
AC Q96BH3; Q96RT0; Q9H4C8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Epididymal sperm-binding protein 1;
DE AltName: Full=Epididymal secretory protein 12;
DE Short=hE12;
DE Flags: Precursor;
GN Name=ELSPBP1; Synonyms=E12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP VARIANT LYS-199.
RX PubMed=11144225;
RX DOI=10.1002/1098-2795(200101)58:1<88::aid-mrd12>3.0.co;2-d;
RA Saalmann A., Muenz S., Ellerbrock K., Ivell R., Kirchhoff C.;
RT "Novel sperm-binding proteins of epididymal origin contain four fibronectin
RT type II-modules.";
RL Mol. Reprod. Dev. 58:88-100(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-199.
RA Luo Y., Zhang X., Yu B.;
RT "A new human homolog 1 of bovine seminal plasma proteins.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-199.
RC TISSUE=Placenta;
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 [5]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17307309; DOI=10.1016/j.gene.2007.01.002;
RA Ekhlasi-Hundrieser M., Schaefer B., Philipp U., Kuiper H., Leeb T.,
RA Mehta M., Kirchhoff C., Toepfer-Petersen E.;
RT "Sperm-binding fibronectin type II-module proteins are genetically linked
RT and functionally related.";
RL Gene 392:253-265(2007).
CC -!- FUNCTION: Binds to spermatozoa upon ejaculation and may play a role in
CC sperm capacitation. Has phosphorylcholine-binding activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11144225,
CC ECO:0000269|PubMed:17307309}.
CC -!- TISSUE SPECIFICITY: Detected in cauda epididymidal fluid and on sperm
CC membrane (at protein level). {ECO:0000269|PubMed:11144225,
CC ECO:0000269|PubMed:17307309}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17307309}.
CC -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC14267.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ278478; CAC14267.1; ALT_FRAME; mRNA.
DR EMBL; AF279147; AAK69481.1; -; mRNA.
DR EMBL; AC010330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015598; AAH15598.1; -; mRNA.
DR CCDS; CCDS12708.1; -.
DR RefSeq; NP_071425.3; NM_022142.4.
DR AlphaFoldDB; Q96BH3; -.
DR SMR; Q96BH3; -.
DR BioGRID; 122060; 127.
DR STRING; 9606.ENSP00000340660; -.
DR DrugBank; DB03945; N,N,N-Trimethyl-2-(phosphonooxy)ethanaminium.
DR GlyGen; Q96BH3; 1 site.
DR iPTMnet; Q96BH3; -.
DR PhosphoSitePlus; Q96BH3; -.
DR BioMuta; ELSPBP1; -.
DR DMDM; 296434494; -.
DR MassIVE; Q96BH3; -.
DR PaxDb; Q96BH3; -.
DR PeptideAtlas; Q96BH3; -.
DR PRIDE; Q96BH3; -.
DR ProteomicsDB; 76076; -.
DR Antibodypedia; 54754; 92 antibodies from 20 providers.
DR DNASU; 64100; -.
DR Ensembl; ENST00000339841.7; ENSP00000340660.2; ENSG00000169393.10.
DR GeneID; 64100; -.
DR KEGG; hsa:64100; -.
DR MANE-Select; ENST00000339841.7; ENSP00000340660.2; NM_022142.5; NP_071425.3.
DR UCSC; uc002pht.4; human.
DR CTD; 64100; -.
DR DisGeNET; 64100; -.
DR GeneCards; ELSPBP1; -.
DR HGNC; HGNC:14417; ELSPBP1.
DR HPA; ENSG00000169393; Tissue enriched (epididymis).
DR MIM; 607443; gene.
DR neXtProt; NX_Q96BH3; -.
DR OpenTargets; ENSG00000169393; -.
DR PharmGKB; PA27765; -.
DR VEuPathDB; HostDB:ENSG00000169393; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000162766; -.
DR InParanoid; Q96BH3; -.
DR OMA; SECIENE; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q96BH3; -.
DR TreeFam; TF343543; -.
DR PathwayCommons; Q96BH3; -.
DR BioGRID-ORCS; 64100; 12 hits in 1074 CRISPR screens.
DR GenomeRNAi; 64100; -.
DR Pharos; Q96BH3; Tbio.
DR PRO; PR:Q96BH3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96BH3; protein.
DR Bgee; ENSG00000169393; Expressed in corpus epididymis and 38 other tissues.
DR ExpressionAtlas; Q96BH3; baseline and differential.
DR Genevisible; Q96BH3; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR CDD; cd00062; FN2; 3.
DR Gene3D; 2.10.10.10; -; 4.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR Pfam; PF00040; fn2; 4.
DR SMART; SM00059; FN2; 4.
DR SUPFAM; SSF57440; SSF57440; 4.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Fertilization; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..223
FT /note="Epididymal sperm-binding protein 1"
FT /id="PRO_0000308249"
FT DOMAIN 25..68
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 69..117
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 124..170
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 177..223
FT /note="Fibronectin type-II 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 88..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 129..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 143..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 182..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 196..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT VARIANT 100
FT /note="C -> W (in dbSNP:rs3745751)"
FT /id="VAR_036760"
FT VARIANT 170
FT /note="D -> N (in dbSNP:rs35362679)"
FT /id="VAR_036761"
FT VARIANT 199
FT /note="E -> K (in dbSNP:rs2303690)"
FT /evidence="ECO:0000269|PubMed:11144225,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_036762"
FT VARIANT 215
FT /note="D -> N (in dbSNP:rs6509358)"
FT /id="VAR_036763"
FT CONFLICT 2
FT /note="T -> N (in Ref. 1; CAC14267)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="V -> A (in Ref. 2; AAK69481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 26106 MW; FC7C215BA3E5CE51 CRC64;
MTRWSSYLLG WTTFLLYSYE SSGGMHEECV FPFTYKGSVY FTCTHIHSLS PWCATRAVYN
GQWKYCQSED YPRCIFPFIY RGKAYNSCIS QGSFLGSLWC SVTSVFDEKQ QWKFCETNEY
GGNSLRKPCI FPSIYRNNVV SDCMEDESNK LWCPTTENMD KDGKWSFCAD TRISALVPGF
PCHFPFNYKN KNYFNCTNEG SKENLVWCAT SYNYDQDHTW VYC
