ID   CRIS3_HORSE             Reviewed;         245 AA.
AC   O19010; Q8HXA1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Cysteine-rich secretory protein 3;
DE            Short=CRISP-3;
DE   AltName: Full=Acidic epididymal glycoprotein 2;
DE            Short=AEG2;
DE   Flags: Precursor;
GN   Name=CRISP3;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Ampulla;
RX   PubMed=9748582; DOI=10.1016/s0167-4838(98)00122-8;
RA   Schambony A., Gentzel M., Wolfes H., Raida M., Neumann U.,
RA   Toepfer-Petersen E.;
RT   "Equine CRISP-3: primary structure and expression in the male genital
RT   tract.";
RL   Biochim. Biophys. Acta 1387:206-216(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Submandibular gland;
RX   PubMed=12459257; DOI=10.1016/s0378-1119(02)01018-1;
RA   Giese A., Jude R., Kuiper H., Raudsepp T., Piumi F., Schambony A.,
RA   Guerin G., Chowdhary B.P., Distl O., Topfer-Petersen E., Leeb T.;
RT   "Molecular characterization of the equine testis-specific protein 1 (TPX1)
RT   and acidic epididymal glycoprotein 2 (AEG2) genes encoding members of the
RT   cysteine-rich secretory protein (CRISP) family.";
RL   Gene 299:101-109(2002).
RN   [3]
RP   INTERACTION WITH A1BG.
RX   PubMed=20116414; DOI=10.1016/j.bbagen.2010.01.011;
RA   Udby L., Johnsen A.H., Borregaard N.;
RT   "Human CRISP-3 binds serum alpha1B-glycoprotein across species.";
RL   Biochim. Biophys. Acta 1800:481-485(2010).
CC   -!- SUBUNIT: Interacts with A1BG. {ECO:0000269|PubMed:20116414}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In neutrophils,
CC       localized in specific granules. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the salivary gland, in the ampulla and
CC       the seminal vesicle. {ECO:0000269|PubMed:12459257,
CC       ECO:0000269|PubMed:9748582}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; AJ001400; CAA04729.1; -; mRNA.
DR   EMBL; AJ459964; CAD31227.1; -; mRNA.
DR   EMBL; AJ459965; CAD31228.1; -; Genomic_DNA.
DR   RefSeq; NP_001075343.1; NM_001081874.1.
DR   AlphaFoldDB; O19010; -.
DR   SMR; O19010; -.
DR   STRING; 9796.ENSECAP00000054102; -.
DR   PaxDb; O19010; -.
DR   GeneID; 100033965; -.
DR   KEGG; ecb:100033965; -.
DR   CTD; 10321; -.
DR   InParanoid; O19010; -.
DR   OrthoDB; 1528782at2759; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0042581; C:specific granule; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR   GO; GO:0009566; P:fertilization; NAS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR   CDD; cd05383; CAP_CRISP; 1.
DR   Gene3D; 1.10.10.740; -; 1.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR042076; Crisp-like_dom.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR013871; Cysteine_rich_secretory.
DR   InterPro; IPR034117; SCP_CRISP.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF08562; Crisp; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..245
FT                   /note="Cysteine-rich secretory protein 3"
FT                   /id="PRO_0000006267"
FT   DOMAIN          42..171
FT                   /note="SCP"
FT   DOMAIN          207..240
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        191..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        194..203
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        207..240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        216..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        225..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   CONFLICT        236
FT                   /note="T -> A (in Ref. 2; CAD31227/CAD31228)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27308 MW;  893A4E87F402BA22 CRC64;
     MALLPVLLFL AAVLLPFFPA SGQDPGFAAL SITKSEVQKE IVNKHNDLRR TVSPLASNML
     KMQWDSKTAT NAQNWANKCL LQHSKAEDRA VGTMKCGENL FMSSIPNSWS DAIQNWHDEV
     HDFKYGVGPK TPNAVVGHYT QVVWYSSYRV GCGIAYCPKQ GTLKYYYVCQ YCPAGNYVNK
     INTPYEQGTP CARCPGNCDN GLCTNSCEYE DLVSNCDSLK KIAGCEHELL KENCKTTCQC
     ENKIY