TX101_RAT
ID TX101_RAT Reviewed; 250 AA.
AC Q924B5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Testis-expressed protein 101 {ECO:0000250|UniProtKB:Q9BY14};
DE AltName: Full=Lipid raft-associated glycoprotein TEC-21;
DE Flags: Precursor;
GN Name=Tex101 {ECO:0000312|RGD:621373};
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], PROTEIN SEQUENCE OF 26-44, FUNCTION,
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Leukemia;
RX PubMed=11809740; DOI=10.1093/intimm/14.2.213;
RA Halova I., Draberova L., Draber P.;
RT "A novel lipid raft-associated glycoprotein, TEC-21, activates rat
RT basophilic leukemia cells independently of the type 1 Fc epsilon
RT receptor.";
RL Int. Immunol. 14:213-223(2002).
CC -!- FUNCTION: Plays a role in fertilization by controlling binding of sperm
CC to zona pellucida and migration of spermatozoa into the oviduct (By
CC similarity). May play a role in signal transduction and promote protein
CC tyrosine phosphorylation (PubMed:11809740).
CC {ECO:0000250|UniProtKB:Q9JMI7, ECO:0000269|PubMed:11809740}.
CC -!- SUBUNIT: Interacts with VAMP3. Interacts with LY6K. Interacts with
CC DPEP3; co-localized on the cell surface of spermatocytes, spermatids,
CC and testicular spermatozoa, co-localized only in cytoplasmic droplets
CC of caput and corpus epididymal sperm. Interacts with ADAM5.
CC {ECO:0000250|UniProtKB:Q9JMI7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11809740};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11809740}. Membrane raft
CC {ECO:0000269|PubMed:11809740}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q9JMI7}. Secreted
CC {ECO:0000250|UniProtKB:Q9JMI7}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9JMI7}. Note=Located on plasma membrane of
CC spermatocytes, round and elongated spermatids, and testicular
CC spermatozoa. {ECO:0000250|UniProtKB:Q9JMI7}.
CC -!- TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|PubMed:11809740}.
CC -!- PTM: N-glycosylated; by high mannose and/or biantennary complex and/or
CC certain types of hybrid oligosaccharides; possesses different
CC oligosaccharides chains according to its subcellular localization in
CC the testis. {ECO:0000269|PubMed:11809740}.
CC -!- PTM: Sheds from membrane raft by ACE and released from the cell surface
CC of epididymal sperm while it passes through the caput epididymis
CC leading to disappearance of TEX101 on spermatozoa; is essential to
CC produce fertile spermatozoa. {ECO:0000250|UniProtKB:Q9JMI7}.
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DR EMBL; AF347056; AAK58911.1; -; mRNA.
DR RefSeq; NP_620606.1; NM_139037.1.
DR AlphaFoldDB; Q924B5; -.
DR SMR; Q924B5; -.
DR STRING; 10116.ENSRNOP00000027202; -.
DR GlyGen; Q924B5; 4 sites.
DR PaxDb; Q924B5; -.
DR PRIDE; Q924B5; -.
DR GeneID; 207113; -.
DR KEGG; rno:207113; -.
DR UCSC; RGD:621373; rat.
DR CTD; 83639; -.
DR RGD; 621373; Tex101.
DR eggNOG; ENOG502T90B; Eukaryota.
DR InParanoid; Q924B5; -.
DR OrthoDB; 1103796at2759; -.
DR PhylomeDB; Q924B5; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q924B5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0002080; C:acrosomal membrane; ISO:RGD.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
DR GO; GO:0031225; C:anchored component of membrane; IDA:RGD.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0009566; P:fertilization; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0002696; P:positive regulation of leukocyte activation; IDA:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
DR GO; GO:1901317; P:regulation of flagellated sperm motility; ISS:UniProtKB.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR Pfam; PF00021; UPAR_LY6; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:11809740"
FT CHAIN 26..224
FT /note="Testis-expressed protein 101"
FT /id="PRO_0000247625"
FT PROPEP 225..250
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000247626"
FT DOMAIN 141..215
FT /note="UPAR/Ly6"
FT LIPID 224
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 250 AA; 27004 MW; CFF31D13C980AC4C CRC64;
MGACRIQYIL LVFLLIASHW TLVQNIYCEV SRTLSLEDNP SGTFNWTSKA EKCNPGEFCQ
ETVLLIKAEG TKTAILASKS CVPQGAETMT FVQYTAPPGL VAISYSNYCN DSLCNNRNNL
ASILQAPEPT ATSNMSGARH CPTCLALEPC SSAPSMPCAN GTTQCYHGKI ELSGGGMDSV
VHVKGCTTAI GCRLMAKMES VGPMTVKETC SYQSFLHPRM AEIGASWMPT SLWVLELLLP
ALSLPLIYFP
