TUTLA_HUMAN
ID TUTLA_HUMAN Reviewed; 1179 AA.
AC Q9P2J2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein turtle homolog A;
DE AltName: Full=Immunoglobulin superfamily member 9A;
DE Short=IgSF9A;
DE Flags: Precursor;
GN Name=IGSF9; Synonyms=IGSF9A, KIAA1355, NRT1;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLU-34 AND
RP THR-1117.
RC TISSUE=Neuroblastoma;
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 DEVELOPMENTAL STAGE.
RX PubMed=11991715; DOI=10.1006/geno.2002.6757;
RA Doudney K., Murdoch J.N., Braybrook C., Paternotte C., Bentley L.,
RA Copp A.J., Stanier P.;
RT "Cloning and characterization of Igsf9 in mouse and human: a new member of
RT the immunoglobulin superfamily expressed in the developing nervous
RT system.";
RL Genomics 79:663-670(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-972, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP STRUCTURE BY NMR OF 624-718.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-008, a FN3 domain in human cDNA.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Functions in dendrite outgrowth and synapse maturation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAGI2 and SHANK1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P2J2-2; O43169: CYB5B; NbExp=3; IntAct=EBI-17451184, EBI-1058710;
CC Q9P2J2-2; Q9NXK6: PAQR5; NbExp=3; IntAct=EBI-17451184, EBI-10316423;
CC Q9P2J2-2; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-17451184, EBI-6656213;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Note=Enriched at
CC the excitatory synapses in mature neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2J2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2J2-2; Sequence=VSP_047195;
CC -!- DEVELOPMENTAL STAGE: Expressed in a wide variety of tissues at 8 and 14
CC weeks of gestation. {ECO:0000269|PubMed:11991715}.
CC -!- DOMAIN: The PDZ-binding motif mediates interactions with MAGI2 and
CC SHANK1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Turtle family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB037776; BAA92593.1; ALT_INIT; mRNA.
DR EMBL; BC030141; AAH30141.1; -; mRNA.
DR CCDS; CCDS1190.1; -. [Q9P2J2-2]
DR CCDS; CCDS44254.1; -. [Q9P2J2-1]
DR RefSeq; NP_001128522.1; NM_001135050.1. [Q9P2J2-1]
DR RefSeq; NP_065840.2; NM_020789.3. [Q9P2J2-2]
DR PDB; 1V5J; NMR; -; A=624-718.
DR PDBsum; 1V5J; -.
DR AlphaFoldDB; Q9P2J2; -.
DR SMR; Q9P2J2; -.
DR BioGRID; 121606; 9.
DR IntAct; Q9P2J2; 6.
DR MINT; Q9P2J2; -.
DR STRING; 9606.ENSP00000357073; -.
DR GlyConnect; 1670; 4 N-Linked glycans (1 site).
DR GlyGen; Q9P2J2; 4 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q9P2J2; -.
DR PhosphoSitePlus; Q9P2J2; -.
DR BioMuta; IGSF9; -.
DR DMDM; 158706515; -.
DR EPD; Q9P2J2; -.
DR jPOST; Q9P2J2; -.
DR MassIVE; Q9P2J2; -.
DR MaxQB; Q9P2J2; -.
DR PaxDb; Q9P2J2; -.
DR PeptideAtlas; Q9P2J2; -.
DR PRIDE; Q9P2J2; -.
DR ProteomicsDB; 83820; -. [Q9P2J2-1]
DR Antibodypedia; 34263; 92 antibodies from 21 providers.
DR DNASU; 57549; -.
DR Ensembl; ENST00000361509.7; ENSP00000355049.3; ENSG00000085552.18. [Q9P2J2-2]
DR Ensembl; ENST00000368094.6; ENSP00000357073.1; ENSG00000085552.18. [Q9P2J2-1]
DR GeneID; 57549; -.
DR KEGG; hsa:57549; -.
DR MANE-Select; ENST00000368094.6; ENSP00000357073.1; NM_001135050.2; NP_001128522.1.
DR UCSC; uc001fuq.2; human. [Q9P2J2-1]
DR CTD; 57549; -.
DR DisGeNET; 57549; -.
DR GeneCards; IGSF9; -.
DR HGNC; HGNC:18132; IGSF9.
DR HPA; ENSG00000085552; Tissue enhanced (liver, retina, skin).
DR MIM; 609738; gene.
DR neXtProt; NX_Q9P2J2; -.
DR OpenTargets; ENSG00000085552; -.
DR PharmGKB; PA38508; -.
DR VEuPathDB; HostDB:ENSG00000085552; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000160444; -.
DR HOGENOM; CLU_008130_2_0_1; -.
DR InParanoid; Q9P2J2; -.
DR OMA; PELGAKT; -.
DR OrthoDB; 291729at2759; -.
DR PhylomeDB; Q9P2J2; -.
DR TreeFam; TF326128; -.
DR PathwayCommons; Q9P2J2; -.
DR SignaLink; Q9P2J2; -.
DR BioGRID-ORCS; 57549; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; IGSF9; human.
DR EvolutionaryTrace; Q9P2J2; -.
DR GenomeRNAi; 57549; -.
DR Pharos; Q9P2J2; Tbio.
DR PRO; PR:Q9P2J2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P2J2; protein.
DR Bgee; ENSG00000085552; Expressed in mucosa of transverse colon and 135 other tissues.
DR ExpressionAtlas; Q9P2J2; baseline and differential.
DR Genevisible; Q9P2J2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR043204; Basigin-like.
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 PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF00041; fn3; 2.
DR SMART; SM00060; FN3; 2.
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 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1179
FT /note="Protein turtle homolog A"
FT /id="PRO_0000306107"
FT TOPO_DOM 21..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..1179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..124
FT /note="Ig-like 1"
FT DOMAIN 136..216
FT /note="Ig-like 2"
FT DOMAIN 226..318
FT /note="Ig-like 3"
FT DOMAIN 322..410
FT /note="Ig-like 4"
FT DOMAIN 418..502
FT /note="Ig-like 5"
FT DOMAIN 507..611
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 623..718
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1177..1179
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 609..626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..919
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C5H6"
FT MOD_RES 972
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 344..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 440..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 321..337
FT /note="YPAQVTAMPPETPLPIG -> C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047195"
FT VARIANT 34
FT /note="G -> E (in dbSNP:rs3747617)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035256"
FT VARIANT 474
FT /note="R -> P (in dbSNP:rs16842846)"
FT /id="VAR_035257"
FT VARIANT 914
FT /note="P -> L (in dbSNP:rs35574000)"
FT /id="VAR_035258"
FT VARIANT 1026
FT /note="S -> T (in dbSNP:rs34749866)"
FT /id="VAR_035259"
FT VARIANT 1117
FT /note="P -> T (in dbSNP:rs1319080)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035260"
FT CONFLICT 279
FT /note="R -> Q (in Ref. 2; AAH30141)"
FT /evidence="ECO:0000305"
FT STRAND 628..634
FT /evidence="ECO:0007829|PDB:1V5J"
FT STRAND 636..644
FT /evidence="ECO:0007829|PDB:1V5J"
FT STRAND 655..662
FT /evidence="ECO:0007829|PDB:1V5J"
FT STRAND 668..674
FT /evidence="ECO:0007829|PDB:1V5J"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:1V5J"
FT STRAND 696..700
FT /evidence="ECO:0007829|PDB:1V5J"
FT STRAND 703..707
FT /evidence="ECO:0007829|PDB:1V5J"
SQ SEQUENCE 1179 AA; 126580 MW; 6C2120D439804407 CRC64;
MVWCLGLAVL SLVISQGADG RGKPEVVSVV GRAGESVVLG CDLLPPAGRP PLHVIEWLRF
GFLLPIFIQF GLYSPRIDPD YVGRVRLQKG ASLQIEGLRV EDQGWYECRV FFLDQHIPED
DFANGSWVHL TVNSPPQFQE TPPAVLEVQE LEPVTLRCVA RGSPLPHVTW KLRGKDLGQG
QGQVQVQNGT LRIRRVERGS SGVYTCQASS TEGSATHATQ LLVLGPPVIV VPPKNSTVNA
SQDVSLACHA EAYPANLTYS WFQDNINVFH ISRLQPRVRI LVDGSLRLLA TQPDDAGCYT
CVPSNGLLHP PSASAYLTVL YPAQVTAMPP ETPLPIGMPG VIRCPVRANP PLLFVSWTKD
GKALQLDKFP GWSQGTEGSL IIALGNEDAL GEYSCTPYNS LGTAGPSPVT RVLLKAPPAF
IERPKEEYFQ EVGRELLIPC SAQGDPPPVV SWTKVGRGLQ GQAQVDSNSS LILRPLTKEA
HGHWECSASN AVARVATSTN VYVLGTSPHV VTNVSVVALP KGANVSWEPG FDGGYLQRFS
VWYTPLAKRP DRMHHDWVSL AVPVGAAHLL VPGLQPHTQY QFSVLAQNKL GSGPFSEIVL
SAPEGLPTTP AAPGLPPTEI PPPLSPPRGL VAVRTPRGVL LHWDPPELVP KRLDGYVLEG
RQGSQGWEVL DPAVAGTETE LLVPGLIKDV LYEFRLVAFA GSFVSDPSNT ANVSTSGLEV
YPSRTQLPGL LPQPVLAGVV GGVCFLGVAV LVSILAGCLL NRRRAARRRR KRLRQDPPLI
FSPTGKSAAP SALGSGSPDS VAKLKLQGSP VPSLRQSLLW GDPAGTPSPH PDPPSSRGPL
PLEPICRGPD GRFVMGPTVA APQERSGREQ AEPRTPAQRL ARSFDCSSSS PSGAPQPLCI
EDISPVAPPP AAPPSPLPGP GPLLQYLSLP FFREMNVDGD WPPLEEPSPA APPDYMDTRR
CPTSSFLRSP ETPPVSPRES LPGAVVGAGA TAEPPYTALA DWTLRERLLP GLLPAAPRGS
LTSQSSGRGS ASFLRPPSTA PSAGGSYLSP APGDTSSWAS GPERWPRREH VVTVSKRRNT
SVDENYEWDS EFPGDMELLE TLHLGLASSR LRPEAEPELG VKTPEEGCLL NTAHVTGPEA
RCAALREEFL AFRRRRDATR ARLPAYRQPV PHPEQATLL
