TUTLB_MOUSE
ID TUTLB_MOUSE Reviewed; 1328 AA.
AC E9PZ19; Q5DU06;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein turtle homolog B;
DE AltName: Full=Immunoglobulin superfamily member 9B {ECO:0000312|MGI:MGI:2685354};
DE Flags: Precursor;
GN Name=Igsf9b {ECO:0000312|MGI:MGI:2685354}; Synonyms=Kiaa1030;
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|Proteomes:UP000000589};
RN [1] {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 [2] {ECO:0000312|EMBL:BAD90425.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-1328.
RC TISSUE=Brain {ECO:0000312|EMBL:BAD90425.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783; SER-794 AND SER-1215,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MAGI2 AND NLGN2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1136, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Transmembrane protein which is abundantly expressed in
CC interneurons, where it may regulate inhibitory synapse development (By
CC similarity). May mediate homophilic cell adhesion (PubMed:23751499).
CC {ECO:0000250|UniProtKB:D3ZB51, ECO:0000269|PubMed:23751499}.
CC -!- SUBUNIT: Found in a complex with MAGI2 and NLGN2, where it interacts
CC with MAGI2 (via PDZ 5 and PDZ 6 domains).
CC {ECO:0000269|PubMed:23751499}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23751499};
CC Single-pass type I membrane protein {ECO:0000255}. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:D3ZB51}; Single-pass type I membrane
CC protein {ECO:0000255}. Postsynaptic density
CC {ECO:0000250|UniProtKB:D3ZB51}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:23751499}.
CC -!- PTM: N-glycosylated and sialylated. Not significantly O-glycosylated.
CC {ECO:0000250|UniProtKB:D3ZB51}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Turtle family.
CC {ECO:0000305}.
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DR EMBL; AC117198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220364; BAD90425.1; -; mRNA.
DR RefSeq; NP_001123259.1; NM_001129787.1.
DR AlphaFoldDB; E9PZ19; -.
DR SMR; E9PZ19; -.
DR IntAct; E9PZ19; 2.
DR MINT; E9PZ19; -.
DR STRING; 10090.ENSMUSP00000117017; -.
DR GlyGen; E9PZ19; 3 sites.
DR iPTMnet; E9PZ19; -.
DR PhosphoSitePlus; E9PZ19; -.
DR MaxQB; E9PZ19; -.
DR PaxDb; E9PZ19; -.
DR PRIDE; E9PZ19; -.
DR ProteomicsDB; 298388; -.
DR Antibodypedia; 2253; 29 antibodies from 12 providers.
DR Ensembl; ENSMUST00000133213; ENSMUSP00000117017; ENSMUSG00000034275.
DR GeneID; 235086; -.
DR UCSC; uc009oqm.2; mouse.
DR CTD; 22997; -.
DR MGI; MGI:2685354; Igsf9b.
DR VEuPathDB; HostDB:ENSMUSG00000034275; -.
DR eggNOG; KOG2408; Eukaryota.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155900; -.
DR HOGENOM; CLU_008169_0_0_1; -.
DR InParanoid; E9PZ19; -.
DR OrthoDB; 291729at2759; -.
DR PhylomeDB; E9PZ19; -.
DR TreeFam; TF326128; -.
DR BioGRID-ORCS; 235086; 1 hit in 72 CRISPR screens.
DR PRO; PR:E9PZ19; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; E9PZ19; protein.
DR Bgee; ENSMUSG00000034275; Expressed in cerebellum lobe and 132 other tissues.
DR ExpressionAtlas; E9PZ19; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0099629; C:postsynaptic specialization of symmetric synapse; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IMP:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Methylation; Neurogenesis; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1328
FT /note="Protein turtle homolog B"
FT /id="PRO_5003245544"
FT TOPO_DOM 18..722
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..1328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 30..115
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 139..226
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 228..320
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 324..415
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 420..504
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 512..604
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 614..708
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 758..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZB51"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZB51"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 161..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 250..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 346..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 442..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1328 AA; 144951 MW; 686913AB14AB2D3D CRC64;
MIWYVATLIA SVISTRGLVA QGAHGLREEP EFVTARAGEG VVLRCDVIHP VTGQPPPYVV
EWFKFGVPIP IFIKFGYYPP HVDPEYAGRA SLHDKASLRL EQVRSEDQGW YECKVLMLDQ
QYDTFHNGSW VHLTINAPPT FTETPPQYIE AKEGGSITMT CTAFGNPKPI VTWLKEGTLL
GASAKYQVSD GSLTVTSVSR EDRGAYTCRA YSIQGEAVHT THLLVQGPPF IVSPPENITV
NISQDALLTC RAEAYPGNLT YTWYWQDENV YFQNDLKLRV RILIDGTLII FRVKPEDAGK
YTCVPSNSLG RSPSASAYLT VQYPARVLNM PPVIYVPVGI HGYIRCPVDA EPPATVVKWN
KDGRPLQVEK NLGWTLMEDG SIRIEEATEE ALGTYTCVPY NTLGTMGQSA PARLVLKDPP
YFTVLPGWEY RQEAGRELLI PCAAAGDPFP VITWRKVGKP SRSKHNALPS GSLQFRALSK
EDHGEWECVA TNVVTSITAS THLTVIGTSP HAPGSVRVHV SMTTANVSWE PGYDGGYEQT
FSVWMKRAQF GPHDWLSLSV PPGPSWLLVD SLEPETAYQF SVLAQNRLGT SAFSEVVTVN
TLAFPVTTPE PLVLVTPPRC LTANRTQQGV LLSWLPPANH SFPIDRYIME FRVGERWEML
DDAIPGTDGD FFAKDLSQDT WYEFRVLAVM QDLISEPSNI AGVSSTDIFP QPDLTDDGLA
RPVLAGIVAT ICFLAAAILF STLAACFVNK QRKRKLKRKK DPPLSITHCR KSLESPLSSG
KVSPESIRTL RAPSESSDDQ GQPAAKRMLS PTREKELSLY KKTKRAISSR KYSVAKAEAE
AEATTPIELI SRGPDGRFVM GPSEMEPSVK GRRIEGFPFA EETDMYPEFR QSDEENEDPL
VPTSVAALKP QLTPMSSSQD SYLPPPAYSP RFQPRGLEGP SGLGGRLQAT GQARPPAPRP
FQHGQYYGYL SSSSPGEVEP PPFYMPEVGS PLSSVMSSPP LHTEGPFGHP TIPEENGENA
SNSTLPLTQT PTGGRSPEPW GRPEFPFGGL ETPAMMFPHQ LHPCDVAESL QPKACLPRGL
PPAPLQVPAA YPGMLSLEAP KGWVGKSPGR GPIPAPPATK WQERPMQPLV SQGQLRHTSQ
GMGIPVLPYP EPAEPGGHGG PSTFGLDTRW YEPQPRPRPS PRQARRAEPS LHQVVLQPSR
LSPLTQSPLS SRTGSPELAA RARPRPGLLQ QAEMSEITLQ PPAAVSFSRK STPSSTGSPS
QSSRSGSPSY RPTMGFTTLA TGYPSPPPGP APPAPGDTLD VFGQTPSPRR MGEEPLRPEP
PTTLPTSG
