GPRL1_MOUSE
ID GPRL1_MOUSE Reviewed; 236 AA.
AC Q9DAG6;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=GLIPR1-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=Glipr1l1 {ECO:0000312|MGI:MGI:1916536};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAB24280.1};
RN [1] {ECO:0000312|EMBL:BAB24280.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB24280.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAB24280.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND GLYCOSYLATION.
RX PubMed=20219979; DOI=10.1210/en.2009-1255;
RA Gibbs G.M., Lo J.C., Nixon B., Jamsai D., O'Connor A.E., Rijal S.,
RA Sanchez-Partida L.G., Hearn M.T., Bianco D.M., O'Bryan M.K.;
RT "Glioma pathogenesis-related 1-like 1 is testis enriched, dynamically
RT modified, and redistributed during male germ cell maturation and has a
RT potential role in sperm-oocyte binding.";
RL Endocrinology 151:2331-2342(2010).
CC -!- FUNCTION: Plays a role in the binding between sperm and oocytes
CC (PubMed:20219979). 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. Also
CC component of the CD9-positive microvesicules found in the cauda region.
CC {ECO:0000250|UniProtKB:Q32LB5, ECO:0000269|PubMed:20219979}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:20219979}. Cell membrane
CC {ECO:0000305|PubMed:20219979}; Peripheral membrane protein
CC {ECO:0000305|PubMed:20219979}; Extracellular side
CC {ECO:0000305|PubMed:20219979}. Membrane raft
CC {ECO:0000250|UniProtKB:Q32LB5}. Secreted {ECO:0000269|PubMed:20219979}.
CC Note=Located in the connecting piece of elongated spermatids and sperm
CC (PubMed:20219979). Also located in the apical region of the sperm head
CC after sperm capacitation (PubMed:20219979). Weakly attached to the cell
CC membrane and later secreted into the extracellular space
CC (PubMed:20219979). 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:0000269|PubMed:20219979}.
CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level). Little or
CC no expression in other tissues tested. {ECO:0000269|PubMed:20219979}.
CC -!- DEVELOPMENTAL STAGE: Detected at postnatal day 14 in developing testis
CC (at protein level). Detected from postnatal day 18 onwards, with
CC increasing levels through to postnatal day 36.
CC {ECO:0000269|PubMed:20219979}.
CC -!- PTM: N-glycosylated (PubMed:20219979). N-glycosylation decreases during
CC the transit in the caput. {ECO:0000250|UniProtKB:Q32LB5,
CC ECO:0000269|PubMed:20219979}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AC159470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK005860; BAB24280.1; -; mRNA.
DR CCDS; CCDS48691.1; -.
DR RefSeq; NP_081294.1; NM_027018.1.
DR AlphaFoldDB; Q9DAG6; -.
DR SMR; Q9DAG6; -.
DR STRING; 10090.ENSMUSP00000073302; -.
DR GlyGen; Q9DAG6; 1 site.
DR PhosphoSitePlus; Q9DAG6; -.
DR PaxDb; Q9DAG6; -.
DR PRIDE; Q9DAG6; -.
DR ProteomicsDB; 267658; -.
DR Ensembl; ENSMUST00000073617; ENSMUSP00000073302; ENSMUSG00000020213.
DR GeneID; 69286; -.
DR KEGG; mmu:69286; -.
DR UCSC; uc007hak.2; mouse.
DR CTD; 256710; -.
DR MGI; MGI:1916536; Glipr1l1.
DR VEuPathDB; HostDB:ENSMUSG00000020213; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000162547; -.
DR HOGENOM; CLU_035730_2_0_1; -.
DR InParanoid; Q9DAG6; -.
DR OMA; SIFVCNY; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q9DAG6; -.
DR TreeFam; TF316148; -.
DR BioGRID-ORCS; 69286; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9DAG6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DAG6; protein.
DR Bgee; ENSMUSG00000020213; Expressed in spermatid and 6 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
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:0097224; C:sperm connecting piece; IDA:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
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; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..236
FT /note="GLIPR1-like protein 1"
FT /id="PRO_5009348226"
FT DOMAIN 46..178
FT /note="SCP"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 236 AA; 27074 MW; 239579A8BF7D1AAA CRC64;
MALKKKLNFL WTLVLYLIAS RLPKAFGKDL PRVPTITDPK FIDAFLNIHN ELRRKVQPPA
ADMNQLFWDQ QLAKLAKAWT RECKLAHNPC IKQRYECLED YDFIGENIYL GRIETQPEDV
VINWYNESKY FNFDFNTCSE MCGHYTQVVW AKTVKIGCAV SNCPNLKGFS AGLFVCNYSP
AGNFIGFRPY TRGDSCSMCG QKTCENSLCR PMNRKTPHHK AACHVLVLGF ILQSLL
