ID   GPRL1_HUMAN             Reviewed;         242 AA.
AC   Q6UWM5; Q96L06;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=GLIPR1-like protein 1;
DE   Flags: Precursor;
GN   Name=GLIPR1L1; ORFNames=UNQ2972/PRO7434;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=16714093; DOI=10.1016/j.ygeno.2006.03.021;
RA   Ren C., Ren C.-H., Li L., Goltsov A.A., Thompson T.C.;
RT   "Identification and characterization of RTVP1/GLIPR1-like genes, a novel
RT   p53 target gene cluster.";
RL   Genomics 88:163-172(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 23-37.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
CC   -!- FUNCTION: Required for optimal fertilization at the stage of sperm-
CC       oocyte fusion, plays a role in optimizing acrosome function, the
CC       translocation of IZUMO1 during the acrosome reaction and the
CC       fertilization process. Component of epididymosomes, one type of
CC       membranous microvesicules which mediate the transfer of lipids and
CC       proteins to spermatozoa plasma membrane during epididymal maturation.
CC       Also component of the CD9-positive microvesicules found in the cauda
CC       region. {ECO:0000250|UniProtKB:Q32LB5, ECO:0000250|UniProtKB:Q9DAG6}.
CC   -!- SUBUNIT: Part of a oolemmal binding multimeric complex (IZUMO1 complex)
CC       composed at least of IZUMO1 and GLIPR1L1; the complex assemblage is
CC       influenced by the maturation status of the male germ cell. Interacts
CC       with IZUMO1. {ECO:0000250|UniProtKB:Q9DAG6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:Q9DAG6}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9DAG6}; Lipid-anchor, GPI-anchor {ECO:0000255};
CC       Extracellular side {ECO:0000250|UniProtKB:Q9DAG6}. Membrane raft
CC       {ECO:0000250|UniProtKB:Q32LB5}. Secreted
CC       {ECO:0000250|UniProtKB:Q9DAG6}. Note=Located in the connecting piece of
CC       elongated spermatids and sperm. Also located in the apical region of
CC       the sperm head after sperm capacitation (By similarity). Weakly
CC       attached to the cell membrane and later secreted into the extracellular
CC       space (By similarity). Located on sperm equatorial segment and neck (By
CC       similarity). Associated with epididymosomes from the caput and cauda
CC       epididymis (By similarity). {ECO:0000250|UniProtKB:Q32LB5,
CC       ECO:0000250|UniProtKB:Q9DAG6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=GLIPR1L1beta;
CC         IsoId=Q6UWM5-1; Sequence=Displayed;
CC       Name=2; Synonyms=GLIPR1L1alpha;
CC         IsoId=Q6UWM5-2; Sequence=VSP_022456;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC       {ECO:0000269|PubMed:16714093}.
CC   -!- PTM: N-glycosylated. N-glycosylation decreases during the transit in
CC       the caput. {ECO:0000250|UniProtKB:Q32LB5}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; AY358731; AAQ89093.1; -; mRNA.
DR   EMBL; BC014603; AAH14603.1; -; mRNA.
DR   CCDS; CCDS76578.1; -. [Q6UWM5-1]
DR   CCDS; CCDS9009.1; -. [Q6UWM5-2]
DR   RefSeq; NP_001291893.1; NM_001304964.1. [Q6UWM5-1]
DR   RefSeq; NP_689992.1; NM_152779.3. [Q6UWM5-2]
DR   AlphaFoldDB; Q6UWM5; -.
DR   SMR; Q6UWM5; -.
DR   BioGRID; 129177; 2.
DR   STRING; 9606.ENSP00000367967; -.
DR   GlyCosmos; Q6UWM5; 1 site, No reported glycans.
DR   GlyGen; Q6UWM5; 1 site.
DR   iPTMnet; Q6UWM5; -.
DR   PhosphoSitePlus; Q6UWM5; -.
DR   BioMuta; GLIPR1L1; -.
DR   DMDM; 124007190; -.
DR   MassIVE; Q6UWM5; -.
DR   PaxDb; 9606-ENSP00000310770; -.
DR   PeptideAtlas; Q6UWM5; -.
DR   ProteomicsDB; 67498; -. [Q6UWM5-1]
DR   ProteomicsDB; 67499; -. [Q6UWM5-2]
DR   Antibodypedia; 29594; 181 antibodies from 25 providers.
DR   DNASU; 256710; -.
DR   Ensembl; ENST00000312442.2; ENSP00000310770.2; ENSG00000173401.10. [Q6UWM5-2]
DR   Ensembl; ENST00000378695.9; ENSP00000367967.4; ENSG00000173401.10. [Q6UWM5-1]
DR   GeneID; 256710; -.
DR   KEGG; hsa:256710; -.
DR   MANE-Select; ENST00000378695.9; ENSP00000367967.4; NM_001304964.2; NP_001291893.1.
DR   UCSC; uc001sxn.4; human. [Q6UWM5-1]
DR   AGR; HGNC:28392; -.
DR   CTD; 256710; -.
DR   DisGeNET; 256710; -.
DR   GeneCards; GLIPR1L1; -.
DR   HGNC; HGNC:28392; GLIPR1L1.
DR   HPA; ENSG00000173401; Tissue enriched (testis).
DR   MIM; 610395; gene.
DR   neXtProt; NX_Q6UWM5; -.
DR   OpenTargets; ENSG00000173401; -.
DR   PharmGKB; PA145008265; -.
DR   VEuPathDB; HostDB:ENSG00000173401; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   GeneTree; ENSGT00940000162547; -.
DR   HOGENOM; CLU_035730_2_0_1; -.
DR   InParanoid; Q6UWM5; -.
DR   OMA; SIFVCNY; -.
DR   OrthoDB; 638273at2759; -.
DR   PhylomeDB; Q6UWM5; -.
DR   TreeFam; TF316148; -.
DR   PathwayCommons; Q6UWM5; -.
DR   BioGRID-ORCS; 256710; 15 hits in 1142 CRISPR screens.
DR   GenomeRNAi; 256710; -.
DR   Pharos; Q6UWM5; Tdark.
DR   PRO; PR:Q6UWM5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q6UWM5; Protein.
DR   Bgee; ENSG00000173401; Expressed in sperm and 97 other cell types or tissues.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
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:0098635; C:protein complex involved in cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISS:UniProtKB.
DR   CDD; cd05385; CAP_GLIPR1-like; 1.
DR   Gene3D; 3.40.33.10; CAP; 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; CYSTEINE-RICH SECRETORY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10334:SF220; GLIPR1-LIKE PROTEIN 1; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00838; V5ALLERGEN.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; PR-1-like; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   Genevisible; Q6UWM5; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW   Direct protein sequencing; Fertilization; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           23..221
FT                   /note="GLIPR1-like protein 1"
FT                   /id="PRO_0000272653"
FT   PROPEP          222..242
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000441107"
FT   DOMAIN          39..171
FT                   /note="SCP"
FT                   /evidence="ECO:0000255"
FT   LIPID           221
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         204..213
FT                   /note="RTPQLIIPNQ -> K (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16714093"
FT                   /id="VSP_022456"
FT   CONFLICT        184
FT                   /note="V -> A (in Ref. 2; AAQ89093)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   242 AA;  27151 MW;  22843450EC652C76 CRC64;
     MALKNKFSCL WILGLCLVAT TSSKIPSITD PHFIDNCIEA HNEWRGKVNP PAADMKYMIW
     DKGLAKMAKA WANQCKFEHN DCLDKSYKCY AAFEYVGENI WLGGIKSFTP RHAITAWYNE
     TQFYDFDSLS CSRVCGHYTQ LVWANSFYVG CAVAMCPNLG GASTAIFVCN YGPAGNFANM
     PPYVRGESCS LCSKEEKCVK NLCRTPQLII PNQNPFLKPT GRAPQQTAFN PFSLGFLLLR
     IF
//