ID   ESPB1_HUMAN             Reviewed;         223 AA.
AC   Q96BH3; Q96RT0; Q9H4C8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-MAR-2009, entry version 43.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=21017566; 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
RT   fibronectin type II-modules.";
RL   Mol. Reprod. Dev. 58:88-100(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
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
RT   linked and functionally related.";
RL   Gene 392:253-265(2007).
CC   -!- FUNCTION: Binds to spermatozoa upon ejaculation and may play a
CC       role in sperm capacitation. Has phosphorylcholine-binding activity
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Detected in cauda epididymidal fluid and on
CC       sperm membrane (at protein level).
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC   -!- SIMILARITY: Contains 4 fibronectin type-II domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC14267.1; Type=Frameshift; Positions=9;
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DR   EMBL; AJ278478; CAC14267.1; ALT_FRAME; mRNA.
DR   EMBL; AF279147; AAK69481.1; -; mRNA.
DR   EMBL; BC015598; AAH15598.1; -; mRNA.
DR   IPI; IPI00059948; -.
DR   RefSeq; NP_071425.2; -.
DR   UniGene; Hs.104894; -.
DR   HSSP; P02784; 1H8P.
DR   PRIDE; Q96BH3; -.
DR   Ensembl; ENSG00000169393; Homo sapiens.
DR   GeneID; 64100; -.
DR   KEGG; hsa:64100; -.
DR   GeneCards; GC19P053189; -.
DR   HGNC; HGNC:14417; ELSPBP1.
DR   MIM; 607443; gene.
DR   PharmGKB; PA27765; -.
DR   HOGENOM; Q96BH3; -.
DR   HOVERGEN; Q96BH3; -.
DR   NextBio; 65932; -.
DR   ArrayExpress; Q96BH3; -.
DR   Bgee; Q96BH3; -.
DR   CleanEx; HS_ELSPBP1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   InterPro; IPR000562; FN_type2_col_bd.
DR   Pfam; PF00040; fn2; 4.
DR   PRINTS; PR00013; FNTYPEII.
DR   ProDom; PD000995; FN_Type_II; 2.
DR   SMART; SM00059; FN2; 4.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 4.
PE   1: Evidence at protein level;
KW   Disulfide bond; Fertilization; Glycoprotein; Polymorphism; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    223       Epididymal sperm-binding protein 1.
FT                                /FTId=PRO_0000308249.
FT   DOMAIN       25     68       Fibronectin type-II 1.
FT   DOMAIN       69    117       Fibronectin type-II 2.
FT   DOMAIN      124    170       Fibronectin type-II 3.
FT   DOMAIN      177    223       Fibronectin type-II 4.
FT   CARBOHYD    195    195       N-linked (GlcNAc...) (Potential).
FT   DISULFID     74    100       By similarity.
FT   DISULFID     88    115       By similarity.
FT   DISULFID    129    153       By similarity.
FT   DISULFID    143    168       By similarity.
FT   DISULFID    182    208       By similarity.
FT   DISULFID    196    223       By similarity.
FT   VARIANT     100    100       C -> W (in dbSNP:rs3745751).
FT                                /FTId=VAR_036760.
FT   VARIANT     170    170       D -> N (in dbSNP:rs35362679).
FT                                /FTId=VAR_036761.
FT   VARIANT     199    199       K -> E (in dbSNP:rs2303690).
FT                                /FTId=VAR_036762.
FT   VARIANT     215    215       D -> N (in dbSNP:rs6509358).
FT                                /FTId=VAR_036763.
FT   CONFLICT      2      2       T -> N (in Ref. 1; CAC14267).
FT   CONFLICT    221    221       V -> A (in Ref. 2; AAK69481).
SQ   SEQUENCE   223 AA;  26105 MW;  F29CCF5BA3E5CE51 CRC64;
     MTRWSSYLLG WTTFLLYSYE SSGGMHEECV FPFTYKGSVY FTCTHIHSLS PWCATRAVYN
     GQWKYCQSED YPRCIFPFIY RGKAYNSCIS QGSFLGSLWC SVTSVFDEKQ QWKFCETNEY
     GGNSLRKPCI FPSIYRNNVV SDCMEDESNK LWCPTTENMD KDGKWSFCAD TRISALVPGF
     PCHFPFNYKN KNYFNCTNKG SKENLVWCAT SYNYDQDHTW VYC
//