TUTLA_RAT
ID TUTLA_RAT Reviewed; 1179 AA.
AC P0C5H6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 FUNCTION.
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP SHANK1.
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Functions in dendrite outgrowth and synapse maturation.
CC {ECO:0000269|PubMed:15340156, ECO:0000269|PubMed:15340157}.
CC -!- SUBUNIT: Interacts with SHANK1 and probably with MAGI2.
CC {ECO:0000269|PubMed:15340156}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15340156};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15340156}.
CC Synapse {ECO:0000269|PubMed:15340156}. Note=Enriched at the excitatory
CC synapses in mature neurons.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal neurons (at protein
CC level). {ECO:0000269|PubMed:15340156}.
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}.
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DR EMBL; AABR03085278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001100667.1; NM_001107197.1.
DR RefSeq; XP_006250352.1; XM_006250290.3.
DR AlphaFoldDB; P0C5H6; -.
DR STRING; 10116.ENSRNOP00000010930; -.
DR GlyGen; P0C5H6; 3 sites.
DR iPTMnet; P0C5H6; -.
DR PhosphoSitePlus; P0C5H6; -.
DR PaxDb; P0C5H6; -.
DR Ensembl; ENSRNOT00000010930; ENSRNOP00000010930; ENSRNOG00000008054.
DR GeneID; 304982; -.
DR KEGG; rno:304982; -.
DR UCSC; RGD:1304566; rat.
DR CTD; 57549; -.
DR RGD; 1304566; Igsf9.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000160444; -.
DR HOGENOM; CLU_008130_2_0_1; -.
DR InParanoid; P0C5H6; -.
DR OMA; PELGAKT; -.
DR OrthoDB; 291729at2759; -.
DR PhylomeDB; P0C5H6; -.
DR TreeFam; TF326128; -.
DR PRO; PR:P0C5H6; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000008054; Expressed in jejunum and 18 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0050807; P:regulation of synapse organization; 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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1179
FT /note="Protein turtle homolog A"
FT /id="PRO_0000306109"
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..498
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 766..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..979
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 /evidence="ECO:0000250"
FT COMPBIAS 793..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 877..895
FT /note="Polar 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:0007744|PubMed:22673903"
FT CARBOHYD 188
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"
SQ SEQUENCE 1179 AA; 127933 MW; 01D777A78F0F1CB9 CRC64;
MIWCLRLTIL SLILSQGADG RRKPEVVSVV GRAGESAVLG CDLLPPAGRP PLHVIEWLRF
GFLLPIFIQF GLYSPRIDPD YVGRVRLQTG ASLQIEGLRV EDQGWYECRV LFLDQHSPEQ
DFANGSWVHL TVNSPPQFQE TPPLVLEVKE LEAVTLRCVA LGSPQPYVTW KFRGQDLGKG
QGQVQVRNGT LWIRRVERGS AGDYTCQASS TEGSVTHTTQ LLVLGPPVIV VPPNNNTVNA
SQDVSLACRA EAYPANLTYS WFQDRINVFH ISRLQSRVRI LVDGSLWLQA TQPDDAGHYT
CVPSNGFPHP PSASAYLTVL YPAQVTVMPP ETPLPIGMRG VIRCPVRANP PLLFVTWTKD
GQALQLDKFP GWSLGPEGSL VIALGNEDAL GEYSCTPYNS LGTAGSSPVT RVLLKAPPAF
IDQPKEEYFQ EVGRDLLIPC SARGDPPPIV SWAKVGRGLQ GQAQVDSNNS LILRPLTKEA
HGRWECSARN AVAHVTISTN VYVLGTSPHV VTNVSVVPLP KGANVSWEPG FDGGYLQRFS
VWYTPLAKRP DRAHHDWVSL AVPMGATHLL VPGLQAYTQY QFSVLAQNKL GSGPFSEIVL
SIPEGLPTTP AVPRLPPTEM PPPLSPPRGL VAVRTPRGVL LHWDPPELIP ERLDGYILEG
RQGSQGWEIL DQGVAGTEIQ LLVPGLIKDV LYEFRLVAFA DSYVSDPSNI ANISTSGLEV
YPSRTQLPGL LPQPVLAGVV GGVCFLGVAV LVSILAACLM NRRRAARRHR KRLRQDPPLI
FSPRGRSGPH SAPGSDSPDS VTKFKLQGSP VPSLRQSLLW GEPARPPSPH PDSPLGRGPL
PLEPICRGPD GRFVMGPTVA PPQEKLCLER SEPRTSAKRL AQSLDCSSSS PSGVPQPLCI
TDISPVGQPP AAMPSPLPGP GPLLQYLSLP FFREMNVDGD WPPLEEPTPA SPPDFMGSHP
CPTSSFLPPP DSPPTNLRAV LPGTLMGVGV SSEPPYTALA DWTLRERVLP GLLSAAPRGS
LTSQSSGRGS ASFLRPPSTA PSAGGSYLSP APGDTSSWAS GPERWPRREH VVTVSKRRNT
SVDENYEWDS EFPGDMELLE TWHPGLASSR AHPELEPELG VKTPEKSCLL NTTHAPGPEA
RCAALREEFL AFRRRRDATR ARLPVCQQSI SYPEQATLL
