TEX2_MOUSE
ID TEX2_MOUSE Reviewed; 1128 AA.
AC Q6ZPJ0; B1ATR1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Testis-expressed protein 2;
GN Name=Tex2; Synonyms=Kiaa1738;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261; SER-264; SER-265 AND
RP SER-749, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-269; SER-294;
RP SER-752; SER-799 AND SER-816, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
CC -!- FUNCTION: During endoplasmic reticulum (ER) stress or when cellular
CC ceramide levels increase, may induce contacts between the ER and
CC medial-Golgi complex to facilitate non-vesicular transport of ceramides
CC from the ER to the Golgi complex where they are converted to complex
CC sphingolipids, preventing toxic ceramide accumulation.
CC {ECO:0000250|UniProtKB:Q8IWB9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q06833}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Enriched at the nucleus-
CC vacuole junction (By similarity). During endoplasmic reticulum (ER)
CC stress, localizes to ER-Golgi contacts (By similarity).
CC {ECO:0000250|UniProtKB:Q06833, ECO:0000250|UniProtKB:Q8IWB9}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC ProRule:PRU01194}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98244.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129434; BAC98244.1; ALT_INIT; mRNA.
DR EMBL; AL663053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25557.1; -.
DR RefSeq; NP_938034.2; NM_198292.3.
DR RefSeq; XP_006533206.1; XM_006533143.3.
DR RefSeq; XP_006533207.1; XM_006533144.3.
DR RefSeq; XP_006533208.1; XM_006533145.1.
DR RefSeq; XP_006533209.1; XM_006533146.3.
DR RefSeq; XP_006533210.1; XM_006533147.3.
DR AlphaFoldDB; Q6ZPJ0; -.
DR BioGRID; 204128; 2.
DR IntAct; Q6ZPJ0; 1.
DR MINT; Q6ZPJ0; -.
DR STRING; 10090.ENSMUSP00000041985; -.
DR GlyGen; Q6ZPJ0; 1 site.
DR iPTMnet; Q6ZPJ0; -.
DR PhosphoSitePlus; Q6ZPJ0; -.
DR EPD; Q6ZPJ0; -.
DR MaxQB; Q6ZPJ0; -.
DR PaxDb; Q6ZPJ0; -.
DR PeptideAtlas; Q6ZPJ0; -.
DR PRIDE; Q6ZPJ0; -.
DR ProteomicsDB; 263108; -.
DR Antibodypedia; 19114; 96 antibodies from 22 providers.
DR Ensembl; ENSMUST00000042780; ENSMUSP00000041985; ENSMUSG00000040548.
DR GeneID; 21763; -.
DR KEGG; mmu:21763; -.
DR UCSC; uc007lzb.1; mouse.
DR CTD; 55852; -.
DR MGI; MGI:102465; Tex2.
DR VEuPathDB; HostDB:ENSMUSG00000040548; -.
DR eggNOG; KOG2238; Eukaryota.
DR GeneTree; ENSGT00390000000463; -.
DR HOGENOM; CLU_008315_0_0_1; -.
DR InParanoid; Q6ZPJ0; -.
DR OMA; IIPLPGY; -.
DR OrthoDB; 332149at2759; -.
DR PhylomeDB; Q6ZPJ0; -.
DR TreeFam; TF314900; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR BioGRID-ORCS; 21763; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Tex2; mouse.
DR PRO; PR:Q6ZPJ0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6ZPJ0; protein.
DR Bgee; ENSMUSG00000040548; Expressed in spermatid and 242 other tissues.
DR ExpressionAtlas; Q6ZPJ0; baseline and differential.
DR Genevisible; Q6ZPJ0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR InterPro; IPR031468; SMP_LBD.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid transport; Lipid-binding;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1128
FT /note="Testis-expressed protein 2"
FT /id="PRO_0000244480"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 817..1102
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWB9"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWB9"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWB9"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWB9"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1128 AA; 125226 MW; 38C2201896B5E479 CRC64;
MTSLNGRHAE KTIDMPKPSA PKVHVQRSVS RDTIAIHFSA SGEEEEEEEE EFRGYLEEGL
DDQSIVTGLE AKEDLYLESQ GGHDPAGPVS TAPADGLSVS ESPAILPVSE NTVKLLESPA
PALQVLSPVP LALSPGSSSS GPLASSPSVS SLSEQKTSSS SPLSSPSKSP VLSSSASSSA
LSSAKPFMSL VKSLSTEVEP KESPHPPRHR HLMKTLVKSL STDTSRQESD TVSYKPPDSK
LNLHLFKQFT QPRNTGGDSK TAPSSPLTSP SDTRSFFKVP EMEAKIEDTK RRLSEVIYEP
FQLLSKIIGE ESGSHRPKAL SASASELSSL SGLNGHLESN NYSIKEEEGD SEGEGYGSDS
NTSRSDHLKP TEDASKEVEP KGSQASSLKD LGLKTSSLVL EKCSLSALVS KEDEEFCELY
TEDFELETEG EGRLDKTLDL PLKPEVLASD GVALESEDEE DSATEHQELP VKTLGFFIMC
VYAYLILPLP YYMSGLFLGV GLGFMTAVCM IWFFTPPSAH KHHKSLKALR HQSTRSLDIK
EPEILKGWMN EIYNYDPETY HATLTHSVFV RLEGGTLRLS KPNKNISRRA SYNETKPEVT
YISQKIYDLS DSKIYLVPKS LARKRIWNKK YPICIELGRQ DDFMSKAQSD KEATEEKPPP
EKELPSEDLK KPPQPQEGTK SSQRDPILYL FGRTGREKEE WFRRFILASR LKSELRKPAG
VSGSKSGLLP AHSRHSSPSG HLSHSRSSSK GSVEEMMSQP KQKELVGSVR QKMLLDYSVY
MGRCVPQDNR SPHRSPVQSA ESSPTASKKL PEAPPSEEEE QEAWVNALLG RIFWDFLGEK
YWSDVVSKKI QMKLSKIKLP YFMNELTLTE LDMGVAVPKI LQAFKPYVDH QGLWIDLEMS
YNGSFLMTLE TKMNLTKLGK EPLVEALKVG EIGKEGCRPR AYCLADSDEE SSSAGSSEED
DPPEPTAGDK QPLPGAEGYV GGHRTSKIMR FVDKITKSKY FQKATETEFI KKKIEEVSNT
PLLLTVEVQE CRGTLAVNIP PPPTDRIWYG FRKPPYVELK ARPKLGEREV TLVHVTEWIE
KKLEQELQKV FVMPNMDDVY IPIMHSAMDP RSTSCLLKEP PVETSDQL
