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SLIK4_MOUSE
ID   SLIK4_MOUSE             Reviewed;         837 AA.
AC   Q810B8; Q8BL56; Q8BWB0; Q8BYG4; Q8C056;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=SLIT and NTRK-like protein 4;
DE   Flags: Precursor;
GN   Name=Slitrk4;
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 {ECO:0000312|EMBL:BAC67207.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14550773; DOI=10.1016/s1044-7431(03)00129-5;
RA   Aruga J., Mikoshiba K.;
RT   "Identification and characterization of Slitrk, a novel neuronal
RT   transmembrane protein family controlling neurite outgrowth.";
RL   Mol. Cell. Neurosci. 24:117-129(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, Olfactory bulb, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   INTERACTION WITH PTPRD.
RX   PubMed=25989451; DOI=10.1038/srep09686;
RA   Yamagata A., Sato Y., Goto-Ito S., Uemura T., Maeda A., Shiroshima T.,
RA   Yoshida T., Fukai S.;
RT   "Structure of Slitrk2-PTPdelta complex reveals mechanisms for splicing-
RT   dependent trans-synaptic adhesion.";
RL   Sci. Rep. 5:9686-9686(2015).
CC   -!- FUNCTION: It is involved in synaptogenesis and promotes synapse
CC       differentiation (By similarity). Suppresses neurite outgrowth
CC       (PubMed:14550773). {ECO:0000250|UniProtKB:Q8IW52,
CC       ECO:0000269|PubMed:14550773}.
CC   -!- SUBUNIT: Interacts (via LRR 1 and 2 repeats) with PTPRD (via
CC       extracellular domain).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8IW52}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:Q8IW52}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q8IW52}.
CC   -!- TISSUE SPECIFICITY: In the adult, significant expression is detected
CC       only in the brain. Broadly expressed in embryonic brain with highest
CC       expression in subventricular zone, subplate, cortical plate, pyramidal
CC       cell layer of hippocampus, thalamus and hypothalamus.
CC       {ECO:0000269|PubMed:14550773}.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, expressed from day 10-12 and
CC       continues through later gestational development and into adulthood.
CC       {ECO:0000269|PubMed:14550773}.
CC   -!- SIMILARITY: Belongs to the SLITRK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC67207.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB097573; BAC67207.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK032263; BAC27786.1; -; mRNA.
DR   EMBL; AK039763; BAC30442.1; -; mRNA.
DR   EMBL; AK053065; BAC35254.1; -; mRNA.
DR   CCDS; CCDS30167.1; -.
DR   RefSeq; NP_848855.2; NM_178740.4.
DR   RefSeq; XP_006528074.1; XM_006528011.1.
DR   RefSeq; XP_006528076.1; XM_006528013.3.
DR   RefSeq; XP_017173974.1; XM_017318485.1.
DR   RefSeq; XP_017173975.1; XM_017318486.1.
DR   RefSeq; XP_017173976.1; XM_017318487.1.
DR   AlphaFoldDB; Q810B8; -.
DR   SMR; Q810B8; -.
DR   BioGRID; 232771; 1.
DR   IntAct; Q810B8; 1.
DR   STRING; 10090.ENSMUSP00000064443; -.
DR   GlyGen; Q810B8; 3 sites.
DR   iPTMnet; Q810B8; -.
DR   PhosphoSitePlus; Q810B8; -.
DR   EPD; Q810B8; -.
DR   MaxQB; Q810B8; -.
DR   PaxDb; Q810B8; -.
DR   PRIDE; Q810B8; -.
DR   ProteomicsDB; 258692; -.
DR   Antibodypedia; 438; 249 antibodies from 32 providers.
DR   DNASU; 245446; -.
DR   Ensembl; ENSMUST00000069926; ENSMUSP00000064443; ENSMUSG00000046699.
DR   Ensembl; ENSMUST00000114679; ENSMUSP00000110327; ENSMUSG00000046699.
DR   GeneID; 245446; -.
DR   KEGG; mmu:245446; -.
DR   UCSC; uc009tio.1; mouse.
DR   CTD; 139065; -.
DR   MGI; MGI:2442509; Slitrk4.
DR   VEuPathDB; HostDB:ENSMUSG00000046699; -.
DR   eggNOG; ENOG502QQXQ; Eukaryota.
DR   GeneTree; ENSGT00940000160971; -.
DR   HOGENOM; CLU_012706_1_0_1; -.
DR   InParanoid; Q810B8; -.
DR   OMA; EPSMFIH; -.
DR   OrthoDB; 217854at2759; -.
DR   PhylomeDB; Q810B8; -.
DR   TreeFam; TF326378; -.
DR   Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR   BioGRID-ORCS; 245446; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Slitrk4; mouse.
DR   PRO; PR:Q810B8; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q810B8; protein.
DR   Bgee; ENSMUSG00000046699; Expressed in lateral septal nucleus and 131 other tissues.
DR   ExpressionAtlas; Q810B8; baseline and differential.
DR   Genevisible; Q810B8; MM.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IEA:InterPro.
DR   GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR043326; Slitrk.
DR   PANTHER; PTHR45773; PTHR45773; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SMART; SM00082; LRRCT; 2.
DR   PROSITE; PS51450; LRR; 12.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..837
FT                   /note="SLIT and NTRK-like protein 4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032680"
FT   TOPO_DOM        19..618
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        619..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        640..837
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          60..81
FT                   /note="LRR 1"
FT   REPEAT          84..105
FT                   /note="LRR 2"
FT   REPEAT          108..129
FT                   /note="LRR 3"
FT   REPEAT          132..153
FT                   /note="LRR 4"
FT   REPEAT          156..177
FT                   /note="LRR 5"
FT   REPEAT          179..200
FT                   /note="LRR 6"
FT   DOMAIN          213..264
FT                   /note="LRRCT 1"
FT   DOMAIN          333..375
FT                   /note="LRRNT"
FT   REPEAT          378..399
FT                   /note="LRR 7"
FT   REPEAT          402..423
FT                   /note="LRR 8"
FT   REPEAT          426..447
FT                   /note="LRR 9"
FT   REPEAT          450..471
FT                   /note="LRR 10"
FT   REPEAT          474..495
FT                   /note="LRR 11"
FT   REPEAT          497..518
FT                   /note="LRR 12"
FT   DOMAIN          531..582
FT                   /note="LRRCT 2"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        429
FT                   /note="R -> G (in Ref. 2; BAC27786)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   837 AA;  94538 MW;  CCD3897E86B95ABC CRC64;
     MFLWLFLIVS ALISSTNADS DISVEICNVC SCVSVENVLY VNCEKVSVYR PNQLKPPWSN
     FYHLNFQNNF LNILYPNTFV NFSHAVSLHL GNNKLQNIEG GAFLGLSALK QLHLNNNELK
     ILRADTFLGI ENLEYLQADY NLIKYIERGA FNKLHKLKVL ILNDNLISFL PDNIFRFASL
     THLDIRGNRI QKLPYIGVLE HIGRVVELQL EDNPWNCSCD LLPLKAWLEN MPYNIYIGEA
     ICETPSDLYG RLLKETNKQE LCPMGTGSDF DVRILPPSQQ ENGFTTPNGH TTQTTLHRLV
     TKPPKTTNPS KISGIVAGKA LSNRNLSQIV SYQTRVPPLT PCPVPCFCKT HPSDLGLSVN
     CQEKNIQSMS ELTPKPLNAK KLHVNGNNIK DVDISDFTEF EGLDLLHLGS NQITLIKGEV
     FHNLTNLRRL YLNGNQIERL YPEIFSGLHN LQYLYLEYNL IKEILAGTFD SMPNLQLLYL
     NNNLLKSLPV YIFSGAPLAR LNLRNNKFMY LPVSGVLDQL QSLTQIDLEG NPWDCTCDLV
     ALKLWLEKLN DGIVVKELKC ETPVQFANIE LKSLKNEILC PKLLNKPSAT FTSPAPAITF
     TTPLGPIRSP PGGPVPLSIL ILSILVVLIL TVFVAFCLLV FVLRRNKKPT VKHEGLGNSE
     CGSMQLQLRK HDHKTNKKDG LSTEAFIPQT IEQMSKSHTC GLKESETGFM FSDPPGQKVM
     MRNAADKDKD LLHVDTRKRL STIDELDELF PSRDSNVFIQ NFLESKKEYN SIGVSGFEIR
     YPEKQQDKKN KKSLIGGNHS KIVVEQRKSE YFELKAKLQS SPDYLQVLEE QTALNKI
 
 
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