GPRL1_BOVIN
ID GPRL1_BOVIN Reviewed; 241 AA.
AC Q32LB5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GLIPR1-like protein 1;
DE Flags: Precursor;
GN Name=GLIPR1L1 {ECO:0000303|PubMed:22552861};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP GPI-ANCHOR, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22552861; DOI=10.1002/jcp.24099;
RA Caballero J., Frenette G., D'Amours O., Belleannee C., Lacroix-Pepin N.,
RA Robert C., Sullivan R.;
RT "Bovine sperm raft membrane associated Glioma Pathogenesis-Related 1-like
RT protein 1 (GliPr1L1) is modified during the epididymal transit and is
RT potentially involved in sperm binding to the zona pellucida.";
RL J. Cell. Physiol. 227:3876-3886(2012).
RN [3]
RP FUNCTION.
RX PubMed=23785420; DOI=10.1371/journal.pone.0065364;
RA Caballero J.N., Frenette G., Belleannee C., Sullivan R.;
RT "CD9-positive microvesicles mediate the transfer of molecules to Bovine
RT Spermatozoa during epididymal maturation.";
RL PLoS ONE 8:E65364-E65364(2013).
CC -!- FUNCTION: Plays a role in the binding between sperm and oocytes
CC (PubMed:22552861). Component of epididymosomes, one type of membranous
CC microvesicules which mediate the transfer of lipids and proteins to
CC spermatozoa plasma membrane during epididymal maturation
CC (PubMed:23785420). Also a component of the CD9-positive microvesicules
CC found in the cauda region (PubMed:23785420).
CC {ECO:0000269|PubMed:22552861, ECO:0000269|PubMed:23785420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q9DAG6}. Cell membrane
CC {ECO:0000269|PubMed:22552861}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:22552861}. Membrane raft
CC {ECO:0000269|PubMed:22552861}. Note=Located in the connecting piece of
CC elongated spermatids and sperm (By similarity). Also located in the
CC apical region of the sperm head after sperm capacitation (By
CC similarity). Located on sperm equatorial segment and neck
CC (PubMed:22552861). Associated with epididymosomes from the caput and
CC cauda epididymis (PubMed:22552861). {ECO:0000250|UniProtKB:Q9DAG6,
CC ECO:0000269|PubMed:22552861}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, where it localizes to
CC round and elongating spermatids and differentiated spermatozoa in the
CC seminiferous tubules and epididymis (at protein level).
CC {ECO:0000269|PubMed:22552861}.
CC -!- PTM: N-glycosylated (PubMed:22552861). N-glycosylation decreases during
CC the transit in the caput. {ECO:0000269|PubMed:22552861}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- CAUTION: Positions of N-glycosylation sites are unclear
CC (PubMed:22552861). No N-glycosylation site is detected by prediction
CC tools. {ECO:0000255, ECO:0000269|PubMed:22552861}.
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DR EMBL; BC109660; AAI09661.1; -; mRNA.
DR RefSeq; NP_001069825.1; NM_001076357.2.
DR AlphaFoldDB; Q32LB5; -.
DR SMR; Q32LB5; -.
DR STRING; 9913.ENSBTAP00000006002; -.
DR PaxDb; Q32LB5; -.
DR Ensembl; ENSBTAT00000006002; ENSBTAP00000006002; ENSBTAG00000004569.
DR GeneID; 615034; -.
DR KEGG; bta:615034; -.
DR CTD; 256710; -.
DR VEuPathDB; HostDB:ENSBTAG00000004569; -.
DR VGNC; VGNC:29403; GLIPR1L1.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000162547; -.
DR HOGENOM; CLU_035730_2_0_1; -.
DR InParanoid; Q32LB5; -.
DR OMA; SIFVCNY; -.
DR OrthoDB; 1528782at2759; -.
DR TreeFam; TF316148; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000004569; Expressed in spermatocyte and 22 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR CDD; cd05385; CAP_GLIPR1-like; 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; IPR001283; CRISP-related.
DR InterPro; IPR034121; SCP_GLIPR-1-like.
DR InterPro; IPR002413; V5_allergen-like.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 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.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Fertilization; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..220
FT /note="GLIPR1-like protein 1"
FT /id="PRO_0000272652"
FT PROPEP 221..241
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441106"
FT DOMAIN 39..172
FT /note="SCP"
FT /evidence="ECO:0000255"
FT LIPID 220
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 241 AA; 27167 MW; FF82324C19B209FC CRC64;
MILRKKLSYL WTLGLCLVAS KSPPKAPSIT NDRFIEECLR LHNEARTNVS PPAADMKYMS
WDEALAKTAE AWAKKCKFIH NSCSSKSFKC HPTFQYAGEN LWLGPLTISA AKFAINMWYD
ERKFYDFNTR SCSQVCGHYT QVVWAYSYKV GCAVAVCPNL GSPDSALLVC NYAPAGNYPN
MSPYTNGTPC SMCQGDTCEN NLCRNKERDK SQRYPNWNPS GTRQLIACNP LYLISVLLTI
F
