TUTLB_HUMAN
ID TUTLB_HUMAN Reviewed; 1349 AA.
AC Q9UPX0; G5EA26;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein turtle homolog B;
DE AltName: Full=Immunoglobulin superfamily member 9B;
DE Short=IgSF9B;
DE Flags: Precursor;
GN Name=IGSF9B; Synonyms=KIAA1030;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 585-1349 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP VARIANTS MET-178 AND LYS-268.
RX PubMed=26506222; DOI=10.1002/ana.24550;
RA Park H.J., Hong Y.B., Choi Y.C., Lee J., Kim E.J., Lee J.S., Mo W.M.,
RA Ki S.M., Kim H.I., Kim H.J., Hyun Y.S., Hong H.D., Nam K., Jung S.C.,
RA Kim S.B., Kim S.H., Kim D.H., Oh K.W., Kim S.H., Yoo J.H., Lee J.E.,
RA Chung K.W., Choi B.O.;
RT "ADSSL1 mutation relevant to autosomal recessive adolescent onset distal
RT myopathy.";
RL Ann. Neurol. 79:231-243(2016).
CC -!- FUNCTION: Transmembrane protein which is abundantly expressed in
CC interneurons, where it may regulate inhibitory synapse development. May
CC mediate homophilic cell adhesion. {ECO:0000250|UniProtKB:D3ZB51,
CC ECO:0000250|UniProtKB:E9PZ19}.
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:0000250|UniProtKB:D3ZB51}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:D3ZB51}; Single-pass type I membrane protein
CC {ECO:0000255}. Postsynaptic density {ECO:0000250|UniProtKB:D3ZB51}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPX0-2; Sequence=VSP_054730;
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; AP000911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB028953; BAA82982.1; -; mRNA.
DR CCDS; CCDS61010.1; -. [Q9UPX0-2]
DR RefSeq; NP_001264214.1; NM_001277285.1. [Q9UPX0-2]
DR AlphaFoldDB; Q9UPX0; -.
DR SMR; Q9UPX0; -.
DR BioGRID; 116644; 3.
DR IntAct; Q9UPX0; 3.
DR MINT; Q9UPX0; -.
DR STRING; 9606.ENSP00000436552; -.
DR GlyGen; Q9UPX0; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPX0; -.
DR PhosphoSitePlus; Q9UPX0; -.
DR BioMuta; IGSF9B; -.
DR DMDM; 158706512; -.
DR EPD; Q9UPX0; -.
DR jPOST; Q9UPX0; -.
DR MassIVE; Q9UPX0; -.
DR PaxDb; Q9UPX0; -.
DR PeptideAtlas; Q9UPX0; -.
DR PRIDE; Q9UPX0; -.
DR ProteomicsDB; 34118; -.
DR ProteomicsDB; 85465; -. [Q9UPX0-1]
DR Antibodypedia; 2253; 29 antibodies from 12 providers.
DR DNASU; 22997; -.
DR Ensembl; ENST00000321016.12; ENSP00000317980.8; ENSG00000080854.16. [Q9UPX0-1]
DR Ensembl; ENST00000533871.8; ENSP00000436552.2; ENSG00000080854.16. [Q9UPX0-2]
DR GeneID; 22997; -.
DR KEGG; hsa:22997; -.
DR MANE-Select; ENST00000533871.8; ENSP00000436552.2; NM_001277285.4; NP_001264214.1. [Q9UPX0-2]
DR UCSC; uc031qfh.2; human. [Q9UPX0-1]
DR CTD; 22997; -.
DR DisGeNET; 22997; -.
DR GeneCards; IGSF9B; -.
DR HGNC; HGNC:32326; IGSF9B.
DR HPA; ENSG00000080854; Tissue enhanced (brain, choroid plexus).
DR MIM; 613773; gene.
DR neXtProt; NX_Q9UPX0; -.
DR OpenTargets; ENSG00000080854; -.
DR PharmGKB; PA142671660; -.
DR VEuPathDB; HostDB:ENSG00000080854; -.
DR eggNOG; KOG2408; Eukaryota.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155900; -.
DR HOGENOM; CLU_008169_0_0_1; -.
DR InParanoid; Q9UPX0; -.
DR OMA; GEAMHTT; -.
DR OrthoDB; 291729at2759; -.
DR PhylomeDB; Q9UPX0; -.
DR TreeFam; TF326128; -.
DR PathwayCommons; Q9UPX0; -.
DR SignaLink; Q9UPX0; -.
DR BioGRID-ORCS; 22997; 7 hits in 941 CRISPR screens.
DR ChiTaRS; IGSF9B; human.
DR GenomeRNAi; 22997; -.
DR Pharos; Q9UPX0; Tdark.
DR PRO; PR:Q9UPX0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UPX0; protein.
DR Bgee; ENSG00000080854; Expressed in right hemisphere of cerebellum and 130 other tissues.
DR ExpressionAtlas; Q9UPX0; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
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: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; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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 InterPro; IPR013106; Ig_V-set.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Methylation; Neurogenesis;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1349
FT /note="Protein turtle homolog B"
FT /id="PRO_0000306110"
FT TOPO_DOM 21..722
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..1349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..129
FT /note="Ig-like 1"
FT DOMAIN 139..226
FT /note="Ig-like 2"
FT DOMAIN 228..320
FT /note="Ig-like 3"
FT DOMAIN 324..415
FT /note="Ig-like 4"
FT DOMAIN 420..504
FT /note="Ig-like 5"
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 911..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1349
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 1195..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1273
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:0000250|UniProtKB:E9PZ19"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PZ19"
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:0000250|UniProtKB:D3ZB51"
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"
FT VAR_SEQ 1329..1349
FT /note="KLQRDRPAPATSPPERALSKL -> TLPPAPGNAAAPERLEALKYQRIKKPK
FT KSSKGSSKSKKRSDDSASQTQQLPNSQVLWPDEAVCLRKKKRHSRPDPFARLSDLCHRQ
FT LPEDQTAILNSVDHDDPGHATLL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054730"
FT VARIANT 178
FT /note="T -> M (in dbSNP:rs77432041)"
FT /evidence="ECO:0000269|PubMed:26506222"
FT /id="VAR_076999"
FT VARIANT 268
FT /note="E -> K (in dbSNP:rs369063193)"
FT /evidence="ECO:0000269|PubMed:26506222"
FT /id="VAR_077000"
FT CONFLICT 1331
FT /note="Q -> R (in Ref. 2; BAA82982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1349 AA; 147089 MW; C8A15ED782EB3893 CRC64;
MIWYVATFIA SVIGTRGLAA EGAHGLREEP EFVTARAGES VVLRCDVIHP VTGQPPPYVV
EWFKFGVPIP IFIKFGYYPP HVDPEYAGRA SLHDKASLRL EQVRSEDQGW YECKVLMLDQ
QYDTFHNGSW VHLTINAPPT FTETPPQYIE AKEGGSITMT CTAFGNPKPI VTWLKEGTLL
GASGKYQVSD GSLTVTSVSR EDRGAYTCRA YSIQGEAVHT THLLVQGPPF IVSPPENITV
NISQDALLTC RAEAYPGNLT YTWYWQDENV YFQNDLKLRV RILIDGTLII FRVKPEDSGK
YTCVPSNSLG RSPSASAYLT VQYPARVLNM PPVIYVPVGI HGYIRCPVDA EPPATVVKWN
KDGRPLQVEK NLGWTLMEDG SIRIEEATEE ALGTYTCVPY NTLGTMGQSA PARLVLKDPP
YFTVLPGWEY RQEAGRELLI PCAAAGDPFP VITWRKVGKP SRSKHSALPS GSLQFRALSK
EDHGEWECVA TNVVTSITAS THLTVIGTSP HAPGSVRVQV SMTTANVSWE PGYDGGYEQT
FSVWMKRAQF GPHDWLSLPV PPGPSWLLVD TLEPETAYQF SVLAQNKLGT SAFSEVVTVN
TLAFPITTPE PLVLVTPPRC LIANRTQQGV LLSWLPPANH SFPIDRYIME FRVAERWELL
DDGIPGTEGE FFAKDLSQDT WYEFRVLAVM QDLISEPSNI AGVSSTDIFP QPDLTEDGLA
RPVLAGIVAT ICFLAAAILF STLAACFVNK QRKRKLKRKK DPPLSITHCR KSLESPLSSG
KVSPESIRTL RAPSESSDDQ GQPAAKRMLS PTREKELSLY KKTKRAISSK KYSVAKAEAE
AEATTPIELI SRGPDGRFVM DPAEMEPSLK SRRIEGFPFA EETDMYPEFR QSDEENEDPL
VPTSVAALKS QLTPLSSSQE SYLPPPAYSP RFQPRGLEGP GGLEGRLQAT GQARPPAPRP
FHHGQYYGYL SSSSPGEVEP PPFYVPEVGS PLSSVMSSPP LPTEGPFGHP TIPEENGENA
SNSTLPLTQT PTGGRSPEPW GRPEFPFGGL ETPAMMFPHQ LPPCDVPESL QPKAGLPRGL
PPTSLQVPAA YPGILSLEAP KGWAGKSPGR GPVPAPPAAK WQDRPMQPLV SQGQLRHTSQ
GMGIPVLPYP EPAEPGAHGG PSTFGLDTRW YEPQPRPRPS PRQARRAEPS LHQVVLQPSR
LSPLTQSPLS SRTGSPELAA RARPRPGLLQ QAEMSEITLQ PPAAVSFSRK STPSTGSPSQ
SSRSGSPSYR PAMGFTTLAT GYPSPPPGPA PAGPGDSLDV FGQTPSPRRT GEELLRPETP
PPTLPTSGKL QRDRPAPATS PPERALSKL
