ID   TX101_CRIGR             Reviewed;         253 AA.
AC   Q7TQN2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
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:0000250|UniProtKB:Q9BY14};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Charvatova L., Tumova M., Draber P.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q924B5, ECO:0000250|UniProtKB:Q9JMI7}.
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:0000250|UniProtKB:Q9JMI7};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9JMI7}. Membrane raft
CC       {ECO:0000250|UniProtKB:Q9JMI7}. 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   -!- 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:0000250|UniProtKB:Q9JMI7}.
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; AY309070; AAP73441.1; -; mRNA.
DR   RefSeq; NP_001233629.1; NM_001246700.1.
DR   AlphaFoldDB; Q7TQN2; -.
DR   SMR; Q7TQN2; -.
DR   GeneID; 100689441; -.
DR   KEGG; cge:100689441; -.
DR   CTD; 83639; -.
DR   OrthoDB; 1103796at2759; -.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IDA:MGI.
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:1901317; P:regulation of flagellated sperm motility; ISS:UniProtKB.
DR   Gene3D; 2.10.60.10; -; 2.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF00021; UPAR_LY6; 2.
DR   SUPFAM; SSF57302; SSF57302; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Repeat; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..226
FT                   /note="Testis-expressed protein 101"
FT                   /id="PRO_0000247619"
FT   PROPEP          227..253
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000247620"
FT   DOMAIN          53..117
FT                   /note="UPAR/Ly6 1"
FT   DOMAIN          143..218
FT                   /note="UPAR/Ly6 2"
FT   LIPID           226
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   253 AA;  26978 MW;  A1BB49698B2589A7 CRC64;
     MAACWVHYLL LLLLGVSHQT LAQSLQCAVS KVLRLEDDPS RTFNWTSKPD KVETCNPGEL
     CQETVLLIKA EGTKTAVVAS KGCASREIEA VTFIQYTPPP GVIAISYSNY CNSSLCNNSK
     NVSLFWKPPD TTATSKILGA LSCPTCVALG SCSSAPSMPC ANSTTQCYQG KIELSGGGMD
     SVLHIKGCTT AIGCRLMAAI TSVGPMTVKE TCSYHSLLQP RKAEESRASG RSTSLWVLEL
     LLPAVLVALT HFP