TUTLA_MOUSE
ID TUTLA_MOUSE Reviewed; 1179 AA.
AC Q05BQ1; Q8R1J8; Q925P4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein turtle homolog A;
DE AltName: Full=Dendrite arborization and synapse maturation protein 1;
DE AltName: Full=Immunoglobulin superfamily member 9A;
DE Short=IgSF9A;
DE Flags: Precursor;
GN Name=Igsf9; Synonyms=Dasm1, Igsf9a, Nrt1;
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 [MRNA] (ISOFORM 1), AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 970-1179 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-83.
RC STRAIN=129S6/SvEvTac;
RX PubMed=11401431; DOI=10.1006/geno.2000.6463;
RA Doudney K., Murdoch J.N., Paternotte C., Bentley L., Gregory S., Copp A.J.,
RA Stanier P.;
RT "Comparative physical and transcript maps of approximately 1 Mb around
RT loop-tail, a gene for severe neural tube defects on distal mouse chromosome
RT 1 and human chromosome 1q22-q23.";
RL Genomics 72:180-192(2001).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15340157; DOI=10.1073/pnas.0405370101;
RA Shi S.-H., Cox D.N., Wang D., Jan L.Y., Jan Y.-N.;
RT "Control of dendrite arborization by an Ig family member, dendrite
RT arborization and synapse maturation 1 (Dasm1).";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13341-13345(2004).
RN [6]
RP FUNCTION, INTERACTION WITH MAGI2 AND SHANK1, AND MUTAGENESIS OF THR-1177.
RX PubMed=15340156; DOI=10.1073/pnas.0405371101;
RA Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.;
RT "The immunoglobulin family member dendrite arborization and synapse
RT maturation 1 (Dasm1) controls excitatory synapse maturation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004).
CC -!- FUNCTION: Functions in dendrite outgrowth and synapse maturation.
CC {ECO:0000269|PubMed:15340156, ECO:0000269|PubMed:15340157}.
CC -!- SUBUNIT: Interacts with MAGI2 and SHANK1.
CC {ECO:0000269|PubMed:15340156}.
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=Q05BQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05BQ1-2; Sequence=VSP_028408, VSP_028409;
CC -!- TISSUE SPECIFICITY: Expressed in both cell bodies and dendrites of
CC cortical and hippocampal neurons and also cerebellar Purkinje cells (at
CC protein level). {ECO:0000269|PubMed:15340157}.
CC -!- DEVELOPMENTAL STAGE: Detected in brain during embryonic development at
CC least from 7.5 dpc until 16.5 dpc. Mainly expressed within the dorsal
CC root glanglia, trigeminal glanglia and olfactory epithelium of 10.5 dpc
CC embryos. Expressed to a lower extent in neuroepithelium, retina and
CC hindgut. {ECO:0000269|PubMed:11991715, ECO:0000269|PubMed:15340157}.
CC -!- DOMAIN: The PDZ-binding motif mediates interactions with MAGI2 and
CC SHANK1.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Turtle family.
CC {ECO:0000305}.
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DR EMBL; AC121551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024487; AAH24487.1; -; mRNA.
DR EMBL; BC034594; AAH34594.1; -; mRNA.
DR EMBL; AF284775; AAK49447.1; -; Genomic_DNA.
DR CCDS; CCDS15515.1; -. [Q05BQ1-1]
DR RefSeq; NP_001139272.1; NM_001145800.1. [Q05BQ1-1]
DR RefSeq; NP_291086.2; NM_033608.3. [Q05BQ1-1]
DR RefSeq; XP_006497119.1; XM_006497056.3. [Q05BQ1-1]
DR AlphaFoldDB; Q05BQ1; -.
DR STRING; 10090.ENSMUSP00000106866; -.
DR GlyGen; Q05BQ1; 5 sites.
DR iPTMnet; Q05BQ1; -.
DR PhosphoSitePlus; Q05BQ1; -.
DR PaxDb; Q05BQ1; -.
DR PRIDE; Q05BQ1; -.
DR ProteomicsDB; 300063; -. [Q05BQ1-1]
DR ProteomicsDB; 300064; -. [Q05BQ1-2]
DR Antibodypedia; 34263; 92 antibodies from 21 providers.
DR DNASU; 93842; -.
DR Ensembl; ENSMUST00000052629; ENSMUSP00000058275; ENSMUSG00000037995. [Q05BQ1-1]
DR Ensembl; ENSMUST00000111235; ENSMUSP00000106866; ENSMUSG00000037995. [Q05BQ1-1]
DR Ensembl; ENSMUST00000127482; ENSMUSP00000117854; ENSMUSG00000037995. [Q05BQ1-2]
DR GeneID; 93842; -.
DR KEGG; mmu:93842; -.
DR UCSC; uc007dqn.2; mouse. [Q05BQ1-1]
DR CTD; 57549; -.
DR MGI; MGI:2135283; Igsf9.
DR VEuPathDB; HostDB:ENSMUSG00000037995; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000160444; -.
DR HOGENOM; CLU_008130_2_0_1; -.
DR InParanoid; Q05BQ1; -.
DR OMA; PELGAKT; -.
DR OrthoDB; 291729at2759; -.
DR PhylomeDB; Q05BQ1; -.
DR TreeFam; TF326128; -.
DR BioGRID-ORCS; 93842; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Igsf9; mouse.
DR PRO; PR:Q05BQ1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q05BQ1; protein.
DR Bgee; ENSMUSG00000037995; Expressed in dorsal pancreas and 167 other tissues.
DR ExpressionAtlas; Q05BQ1; baseline and differential.
DR Genevisible; Q05BQ1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IMP:MGI.
DR GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:MGI.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
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 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_0000306108"
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 767..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1177..1179
FT /note="PDZ-binding"
FT COMPBIAS 788..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..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 CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
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 505..528
FT /note="GTSPHVVTNVSVVPLPKGANVSWE -> EPSVLTEPTMTGYLWLCLSGLHTS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028408"
FT VAR_SEQ 529..1179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028409"
FT MUTAGEN 1177
FT /note="T->A: Loss of interaction with MAGI2 and SHANK1 and
FT loss of function."
FT /evidence="ECO:0000269|PubMed:15340156"
FT CONFLICT 49
FT /note="H -> R (in Ref. 4; AAK49447)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="A -> V (in Ref. 3; AAH24487)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1179 AA; 127330 MW; 8CD76F4D1B32A2DF CRC64;
MIWCLRLTVL SLIISQGADG RRKPEVVSVV GRAGESAVLG CDLLPPAGHP PLHVIEWLRF
GFLLPIFIQF GLYSPRIDPD YVGRVRLQTG ASLQIEGLRV EDQGWYECRV LFLDQHSPEQ
DFANGSWVHL TVNSPPQFQE TPPLVLEVKE LEAVTLRCVA RGSPQPYVTW KFRGQDLGKG
QGQVQVQNGT LWIRRVERGS AGDYTCQASS SEGSITHATQ LLVLGPPVIV VPPSNSTVNS
SQDVSLACRA EAYPANLTYS WFQDGVNVFH ISRLQSRVRI LVDGSLWLQA TQPDDAGHYT
CVPSNGFLHP PSASAYLTVL YPAQVTVMPP ETPLPTGMRG VIRCPVRANP PLLFVTWTKD
GQALQLDKFP GWSLGPEGSL IIALGNENAL GEYSCTPYNS LGTAGPSPVT QVLLKAPPAF
IDQPKEEYFQ EVGRELLIPC SARGDPPPIV SWAKVGRGLQ GQAQVDSNNS LVLRPLTKEA
QGRWECSASN AVARVTTSTN VYVLGTSPHV VTNVSVVPLP KGANVSWEPG FDGGYLQRFS
VWYTPLAKRP DRAHHDWVSL AVPIGATHLL VPGLQAHAQY QFSVLAQNKL GSGPFSEIVL
SIPEGLPTTP AAPGLPPTEI PPPLSPPRGL VAVRTPRGVL LHWDPPELIP GRLDGYILEG
RQGSQGWEIL DQGVAGTEIQ LLVPGLIKDV LYEFRLVAFA DSYVSDPSNV ANISTSGLEV
YPSRTQLPGL LPQPVLAGVV GGVCFLGVAV LVSILAACLM NRRRAARRHR KRLRQDPPLI
FSPRGKSGSH SAPGSGSPDS VTKFKLQGSP VPSLRQSLLW GEPARPPSPH PDSPLGRGPL
PLEPICRGPD GRFVMGPTVA PSQEKLCLER SEPRTSAKRL AQSFDCSSSS PSGVPQPLCI
TDISPVGQPL AAVPSPLPGP GPLLQYLSLP FFREMNVDGD WPPLEEPTPA PPPDFMDSQP
CPTSSFLPPP DSPPANLRAV LPGTLMGVGV SSEPPYTALA DWTLRERVLP GLLSAAPRGS
LTSQSSGRGS ASFLRPPSTA PSAGGSYLSP APGDTSSWAS GPERWPRREH VVTVSKRRNT
SVDENYEWDS EFPGDMELLE TWHPGLASSR THPELEPELG VKTPEESCLL NPTHAAGPEA
RCAALREEFL AFRRRRDATR ARLPAYQQSI SYPEQATLL
