CRIS1_RAT
ID CRIS1_RAT Reviewed; 246 AA.
AC P12020;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cysteine-rich secretory protein 1;
DE AltName: Full=32 kDa epididymal protein;
DE AltName: Full=Acidic epididymal glycoprotein;
DE Short=Protein D;
DE Short=Protein E;
DE AltName: Full=Protein IV;
DE AltName: Full=Sialoprotein;
DE AltName: Full=Sperm-coating glycoprotein;
DE Short=SCP;
DE Flags: Precursor;
GN Name=Crisp1; Synonyms=Aeg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=3780731; DOI=10.1111/j.1432-1033.1986.tb10118.x;
RA Brooks D.E., Means A.R., Wright E.J., Singh S.P., Tiver K.K.;
RT "Molecular cloning of the cDNA for androgen-dependent sperm-coating
RT glycoproteins secreted by the rat epididymis.";
RL Eur. J. Biochem. 161:13-18(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2460753; DOI=10.1210/mend-2-10-999;
RA Charest N.J., Joseph D.R., Wilson E.M., French F.S.;
RT "Molecular cloning of complementary deoxyribonucleic acid for an androgen-
RT regulated epididymal protein: sequence homology with metalloproteins.";
RL Mol. Endocrinol. 2:999-1004(1988).
CC -!- FUNCTION: This protein is supposed to help spermatozoa undergo
CC functional maturation while they move from the testis to the ductus
CC deferens.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Secreted by the epididymal epithelium and then
CC becomes associated with the sperm surface.
CC -!- INDUCTION: By androgens.
CC -!- PTM: Two major variant protein D and E differ from each other by their
CC carbohydrate side chains.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; X04643; CAA28304.1; -; mRNA.
DR EMBL; M31173; AAB59716.1; -; mRNA.
DR PIR; A40918; A24609.
DR RefSeq; NP_074050.1; NM_022859.1.
DR RefSeq; XP_017452115.1; XM_017596626.1.
DR AlphaFoldDB; P12020; -.
DR SMR; P12020; -.
DR STRING; 10116.ENSRNOP00000018162; -.
DR GlyGen; P12020; 3 sites.
DR PaxDb; P12020; -.
DR Ensembl; ENSRNOT00000018163; ENSRNOP00000018162; ENSRNOG00000013496.
DR GeneID; 64827; -.
DR KEGG; rno:64827; -.
DR UCSC; RGD:619846; rat.
DR CTD; 10321; -.
DR RGD; 619846; Crisp1.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000162013; -.
DR HOGENOM; CLU_035730_2_1_1; -.
DR InParanoid; P12020; -.
DR OMA; IANCGEN; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; P12020; -.
DR TreeFam; TF316148; -.
DR PRO; PR:P12020; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000013496; Expressed in esophagus and 6 other tissues.
DR Genevisible; P12020; RN.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; ISO:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..246
FT /note="Cysteine-rich secretory protein 1"
FT /id="PRO_0000006263"
FT DOMAIN 46..172
FT /note="SCP"
FT DOMAIN 208..241
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 192..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 195..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 208..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 217..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 226..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 246 AA; 27847 MW; 585207C7CF7CF9D1 CRC64;
MALMLVLLFL AAVLPPSLLQ DTTDEWDRDL ENLSTTKLSV QEEIINKHNQ LRRTVSPSGS
DLLRVEWDHD AYVNAQKWAN RCIYNHSPLQ HRTTTLKCGE NLFMANYPAS WSSVIQDWYD
ESLDFVFGFG PKKVGVKVGH YTQVVWNSTF LVACGVAECP DQPLKYFYVC HYCPGGNYVG
RLYSPYTEGE PCDSCPGNCE DGLCTNSCEY EDNYSNCGDL KKMVSCDDPL LKEGCRASCF
CEDKIH
