T131L_MOUSE
ID T131L_MOUSE Reviewed; 1597 AA.
AC Q3U3D7; Q6P5E2; Q6PHM5; Q6ZQ24; Q8C2B9; Q8K2U7; Q8R3Y2; Q8R580;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Transmembrane protein 131-like;
DE Flags: Precursor;
GN Name=Tmem131l {ECO:0000250|UniProtKB:A2VDJ0};
GN Synonyms=Kiaa0922 {ECO:0000250|UniProtKB:A2VDJ0};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 654-1597 (ISOFORM 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-1597 (ISOFORM 2).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: In its membrane-associated form, antagonizes canonical Wnt
CC signaling by triggering lysosome-dependent degradation of Wnt-activated
CC LRP6. Regulates thymocyte proliferation.
CC {ECO:0000250|UniProtKB:A2VDJ0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A2VDJ0};
CC Single-pass type I membrane protein {ECO:0000305}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:A2VDJ0}. Cytoplasm
CC {ECO:0000250|UniProtKB:A2VDJ0}. Note=During intrathymic development,
CC resides in punctate cytoplasmic structures in DN1 and DN2 cells. In DN3
CC cells, found in large crescent-shaped membrane structures, which
CC preferentially localize in cell-to-cell contact zones.
CC {ECO:0000250|UniProtKB:A2VDJ0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U3D7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U3D7-2; Sequence=VSP_032833;
CC Name=3;
CC IsoId=Q3U3D7-3; Sequence=VSP_032832, VSP_032833, VSP_032834;
CC -!- SIMILARITY: Belongs to the TMEM131 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29771.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC Sequence=AAH62940.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40642.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK088900; BAC40642.1; ALT_INIT; mRNA.
DR EMBL; AK154818; BAE32851.1; -; mRNA.
DR EMBL; BC023166; AAH23166.1; -; mRNA.
DR EMBL; BC023391; AAH23391.1; -; mRNA.
DR EMBL; BC029771; AAH29771.1; ALT_SEQ; mRNA.
DR EMBL; BC056491; AAH56491.1; -; mRNA.
DR EMBL; BC062940; AAH62940.1; ALT_INIT; mRNA.
DR EMBL; AK129240; BAC98050.1; -; mRNA.
DR CCDS; CCDS38463.1; -. [Q3U3D7-1]
DR RefSeq; NP_766269.3; NM_172681.4. [Q3U3D7-1]
DR RefSeq; XP_006501388.1; XM_006501325.1. [Q3U3D7-2]
DR AlphaFoldDB; Q3U3D7; -.
DR STRING; 10090.ENSMUSP00000049808; -.
DR GlyGen; Q3U3D7; 4 sites.
DR iPTMnet; Q3U3D7; -.
DR PhosphoSitePlus; Q3U3D7; -.
DR MaxQB; Q3U3D7; -.
DR PaxDb; Q3U3D7; -.
DR PeptideAtlas; Q3U3D7; -.
DR PRIDE; Q3U3D7; -.
DR ProteomicsDB; 254517; -. [Q3U3D7-1]
DR ProteomicsDB; 254518; -. [Q3U3D7-2]
DR ProteomicsDB; 254519; -. [Q3U3D7-3]
DR Antibodypedia; 57011; 59 antibodies from 11 providers.
DR DNASU; 229473; -.
DR Ensembl; ENSMUST00000191758; ENSMUSP00000141438; ENSMUSG00000033767. [Q3U3D7-1]
DR Ensembl; ENSMUST00000192095; ENSMUSP00000141607; ENSMUSG00000033767. [Q3U3D7-3]
DR GeneID; 229473; -.
DR KEGG; mmu:229473; -.
DR UCSC; uc008ppo.1; mouse. [Q3U3D7-2]
DR UCSC; uc008ppp.1; mouse. [Q3U3D7-1]
DR UCSC; uc008ppq.1; mouse. [Q3U3D7-3]
DR CTD; 23240; -.
DR MGI; MGI:2443399; Tmem131l.
DR VEuPathDB; HostDB:ENSMUSG00000033767; -.
DR eggNOG; KOG3620; Eukaryota.
DR GeneTree; ENSGT00530000063614; -.
DR HOGENOM; CLU_004094_0_0_1; -.
DR InParanoid; Q3U3D7; -.
DR OMA; HNGFPCP; -.
DR OrthoDB; 45814at2759; -.
DR PhylomeDB; Q3U3D7; -.
DR TreeFam; TF321435; -.
DR BioGRID-ORCS; 229473; 4 hits in 72 CRISPR screens.
DR ChiTaRS; D930015E06Rik; mouse.
DR PRO; PR:Q3U3D7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3U3D7; protein.
DR Bgee; ENSMUSG00000033767; Expressed in ventricular zone and 247 other tissues.
DR ExpressionAtlas; Q3U3D7; baseline and differential.
DR Genevisible; Q3U3D7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR039877; TMEM131-like.
DR InterPro; IPR045695; TMEM131-like_conserved.
DR InterPro; IPR022113; TMEM131-like_N.
DR PANTHER; PTHR22050; PTHR22050; 1.
DR Pfam; PF19532; TMEM131_like; 1.
DR Pfam; PF12371; TMEM131_like_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..1597
FT /note="Transmembrane protein 131-like"
FT /id="PRO_0000328866"
FT TOPO_DOM 41..869
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 891..1597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 696..916
FT /note="Required for Wnt-signaling inhibition and LRP6
FT degradation"
FT /evidence="ECO:0000250|UniProtKB:A2VDJ0"
FT REGION 907..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 929..930
FT /note="KS -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032832"
FT VAR_SEQ 1275..1335
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032833"
FT VAR_SEQ 1430
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032834"
FT CONFLICT 357
FT /note="S -> L (in Ref. 3; BAC98050)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="K -> R (in Ref. 3; BAC98050)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="Q -> H (in Ref. 3; BAC98050)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="S -> A (in Ref. 3; BAC98050)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="I -> S (in Ref. 2; AAH62940)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="M -> I (in Ref. 2; AAH23391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="S -> P (in Ref. 2; AAH23391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1081
FT /note="Y -> C (in Ref. 2; AAH23391)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="R -> G (in Ref. 1; BAC40642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1257
FT /note="K -> T (in Ref. 2; AAH23391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1597 AA; 175772 MW; A1EEEAA94AD2FA20 CRC64;
MAGLRRPQSG AYRRTAAAVN LLLGVFQVLL SCCRPGGAQG QAFEPLPNVV ELWQAEEGEL
LLPTQGDSEE DMEEPSQEQS FSDKLFIGKG LHFQPSVLDF GIQFLGHPAA KLLYAYNPSR
ESEVVVNSVF TAARHFHVPP VHCRVIPAMG KASFRVIFLP TEEGSIESSL FINTSSHGVF
SYHVSGVGTR RVSTEGSAEQ LPNAYFLLPQ VQSIQLSQTQ AETTNTSLLR VQLECSLHNK
VCQQLKSCSL GSDDALHLEM NIIVAVENSS KQPEENTQAL LDHLSIVYVA TDESDTSDES
AVNMYVLHSG NSLIWIQDIH HFSQKNVLSL QFEPVLLSTS TTNFTKIASF TCKAGTSCDS
GIMGLRKKKA SPAMQACLSS PVVQGYFRTD ASTAQFHIES HETATGVWSI WYRSHFDQSI
VLKDVFVSKE TKHILKVLSF RGPLFLPPGC WNIFSLKLAV KGIVLNLFTN VFLTTNTGAI
FAIPLQIFSA PTKEGSLGFE VLAHCGMHYF MGKSKTENPN WERSLSLDRS TWDMDSELAN
KLYERWKKYK SGDACRRNVL GMSQFAFTKK SKETEPFVSF LPRVVPEPNL VLNFSATALR
NSAVKYFVVR NPTPQPVSLQ LLPLSLYPRP EAAVRLLHKW FGTDMQMVNL STGEFQLTQA
CPYQGEPSEE SSLGALHVHL QALETRRVGV VFTPADYGKV TSLILIRNNL TVVDMVGVEG
FGAQELLKVG GRLPGAGGSL RFKVPESTLM DCHRQLKDSK QILSITKNFK VENIGPLPIT
VTSLKINGYN CQGYGFEVLD CHPFSLSPNT SRDISIVFTP DFTSSWVIRE LTLVTAADLE
FHFTLNVTLP HHMLPLCAEV VPGPSWEESF WRLTVFFVSL SLLGVILIAF QQAQYILMEF
MKTRQRQNGS SSSQQNGDPV AMISSHPHKS TCKNFLDTYS PSDKGRGKSC LPVGPSLSRL
QNAAKRSPAT YGHSQKKHKC SFYYSKQKPS ASAASSANVT TEEKQTVTLA SSLSVAKEDI
CTNVLSENWV SLRYASGING SLQKNLTLPK NVLHKEESSL KNTVVTNTPS ECSMKEGVHT
YMFPKETDSK ISENVAELKE QEPCPQKTSK KPPESTLPKT PPQYLQSDLP EVSRKHGNKQ
QAPVRSEVDS FEPVRAADAE PSSVRKTQGA SPEDTCSEKQ DTPSAEQEDP SRKRKLQERR
EGSTQALNWN KTRPCRRNKK RASAQASSSP RPSEQSEQRL VCSDVRSWCA QDGAGEKCKA
GTEVSGSSPE RREEDSYYQK SEKKCADKFC SDSSSDCGSS SGSVRASRGS WGSWSSSSSD
CDRRPVVDIQ HFLPPGDGVS PQNFPSEASV PLSLPQHVCS STDVSVLPEF TESPCPGLPA
TPAGAGEEKG LYPPGGLWPS QPVCLTSSFN CPVENGAPGV SQEPTSIPDS SFIDWSASCE
GQFPSVYCPL ELNDYNAFPE ENMNYTNGFP CSSKVQTDFI GHSTPSTWNT PASMPAAWGH
ASLVNSPSYL TSTRSLSPMS GLFGSIWAPQ SEVYETCCPI SPATEHATHM ENQVMCKEYY
LGFNPFRAYM NLDIWTSTAN RNANFPLSRD SSYCGNM
