TUTLB_RAT
ID TUTLB_RAT Reviewed; 1328 AA.
AC D3ZB51;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein turtle homolog B;
DE AltName: Full=Immunoglobulin superfamily member 9B {ECO:0000312|RGD:1564717};
DE Flags: Precursor;
GN Name=Igsf9b {ECO:0000312|RGD:1564717};
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 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775; SER-783; SER-794 AND
RP SER-1207, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MAGI2 AND NLGN2, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
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).
CC -!- FUNCTION: Transmembrane protein which is abundantly expressed in
CC interneurons, where it may regulate inhibitory synapse development
CC (PubMed:23751499). May mediate homophilic cell adhesion (By
CC similarity). {ECO:0000250|UniProtKB:E9PZ19,
CC 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: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:23751499}; Single-pass membrane protein
CC {ECO:0000255}. Postsynaptic density {ECO:0000269|PubMed:23751499}.
CC -!- TISSUE SPECIFICITY: Detected primarily in brain, including cortex,
CC hippocampus, cerebellum and striatum. Largely restricted to inhibitory
CC GABAergic interneurons (at protein level).
CC {ECO:0000269|PubMed:23751499}.
CC -!- DEVELOPMENTAL STAGE: Expression in brain gradually increases from
CC postnatal day 1 onwards and reaches maximum levels by postnatal week 3.
CC {ECO:0000269|PubMed:23751499}.
CC -!- PTM: N-glycosylated and sialylated. Not significantly O-glycosylated.
CC {ECO:0000269|PubMed:23751499}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Turtle family.
CC {ECO:0000305}.
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DR EMBL; AABR07069538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; D3ZB51; -.
DR SMR; D3ZB51; -.
DR CORUM; D3ZB51; -.
DR STRING; 10116.ENSRNOP00000012391; -.
DR GlyGen; D3ZB51; 3 sites.
DR iPTMnet; D3ZB51; -.
DR PhosphoSitePlus; D3ZB51; -.
DR PaxDb; D3ZB51; -.
DR PRIDE; D3ZB51; -.
DR UCSC; RGD:1564717; rat.
DR RGD; 1564717; Igsf9b.
DR VEuPathDB; HostDB:ENSRNOG00000009253; -.
DR eggNOG; KOG2408; Eukaryota.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_008169_0_0_1; -.
DR InParanoid; D3ZB51; -.
DR OMA; GEAMHTT; -.
DR PhylomeDB; D3ZB51; -.
DR TreeFam; TF326128; -.
DR PRO; PR:D3ZB51; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000009253; Expressed in frontal cortex and 9 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; ISO:RGD.
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; ISO:RGD.
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; IDA:SynGO.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1328
FT /note="Protein turtle homolog B"
FT /id="PRO_5003052708"
FT TOPO_DOM 21..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 1107..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:0007744|PubMed:22673903"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9PZ19"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PZ19"
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; 145079 MW; 67FD7B1F19117461 CRC64;
MIWYVATLIA SVISTRGLVA QVAHGLREEP EFVTARAGEG VVLRCDVIHP VTGQPPPYVV
EWFKFGVPIP IFIKFGYYPP HVDPEYAGRA SLHDKASLRL EQVRSEDQGW YECKVLMLDQ
QYDTFHNGSW VHLTINAPPT FTETPPQYIE AKEGGSITMT CTAFGNPKPI VTWLKEGTLL
SASGKYQVSD 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 PLGPSWLLVD SLEPETAYQF SVLAQNRLGT SAFSEVVTVN
TLAFPVTTPE PLVLVTPPRC LTANRTQQGV LLSWLPPANH SFPIDRYIME FRVGERWEML
DDAIPGTDGE 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 QPKPCLPRGL
PPAPLQVPAA YPGMLSLEAP KGWVGKSPGR GPIPAPPATK WQERPMQPLV SQGQLRHTSQ
GMGIPVLPYP EPAEPGGHGG PSTFGLDTRW YEPQPRPRPS PRQARRAEPS LHQVVLQPSR
LSPLTQSPLS SRTGSPELAA RARPRPGLLQ QAEMSEITLQ PPAAVSFSRK STPSSTGSPS
QSSRSGSPSY RPTMGFTTLA TGYPSPPPGP APPAPGDNLD VFGQTPSPRR MGEEPLRPEP
PTTLPTSG
