ID   CRIS1_MACMU             Reviewed;         249 AA.
AC   Q9XSD3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cysteine-rich secretory protein 1;
DE            Short=CRISP-1;
DE   AltName: Full=Androgen-dependent acidic epididymal glycoprotein;
DE            Short=AEG;
DE   AltName: Full=mAEG;
DE   Flags: Precursor;
GN   Name=CRISP1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=10386818;
RA   Sivashanmugam P., Richardson R.T., Hall S., Hamil K.G., French F.S.,
RA   O'Rand M.G.;
RT   "Cloning and characterization of an androgen-dependent acidic epididymal
RT   glycoprotein/CRISP1-like protein from the monkey.";
RL   J. Androl. 20:384-393(1999).
CC   -!- FUNCTION: May have a role in sperm-egg fusion and maturation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Note=Located in the lumen and epithelium of
CC       distal ductus efferentes and epididymal ducts, and on the postacrosomal
CC       region of the sperm head. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in all the regions of the epididymis
CC       except the caput and is not detected in the testis, prostate, seminal
CC       vesicle, and brain. {ECO:0000269|PubMed:10386818}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; AF123894; AAD27611.1; -; mRNA.
DR   RefSeq; NP_001027983.1; NM_001032811.1.
DR   AlphaFoldDB; Q9XSD3; -.
DR   SMR; Q9XSD3; -.
DR   STRING; 9544.ENSMMUP00000005602; -.
DR   GeneID; 574111; -.
DR   KEGG; mcc:574111; -.
DR   CTD; 167; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   HOGENOM; CLU_035730_2_1_1; -.
DR   InParanoid; Q9XSD3; -.
DR   OMA; YDEYTDC; -.
DR   OrthoDB; 1528782at2759; -.
DR   TreeFam; TF316148; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
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   InterPro; IPR002413; V5_allergen-like.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF08562; Crisp; 1.
DR   PRINTS; PR00838; V5ALLERGEN.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..249
FT                   /note="Cysteine-rich secretory protein 1"
FT                   /id="PRO_0000006261"
FT   DOMAIN          45..175
FT                   /note="SCP"
FT   DOMAIN          211..244
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        195..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        198..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        211..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        220..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        229..242
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   249 AA;  28653 MW;  26DD3071C5F1F2A1 CRC64;
     MEIKHLLFLV AAACLLPVLS MKRKSAKKLF NKLVTDLPNV QQEIVNIHNT LRRGVVPPAS
     NMLKMSWSEE AAQNAKIFSR YCDMTESNPL ERRLPNTFCG ENRNMTSYPV SWSSVIGVWY
     SESKYFRYGL WPSTDDDIST DRYTQIVWAT SYLIGCAIAP CRHRGSPRYF YVCHYCHEGN
     DPETKHEPYK KGVPCEACPN NCEDKLCTNP CIYYDEYTDC SLEVRFLGCN HSTPRMFCKA
     TCLCDTEIK