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SLIK2_HUMAN
ID   SLIK2_HUMAN             Reviewed;         845 AA.
AC   Q9H156; A8K117; Q2KHN3; Q5JXB1; Q8NBC7; Q96JH3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=SLIT and NTRK-like protein 2;
DE   Flags: Precursor;
GN   Name=SLITRK2; Synonyms=CXorf2, KIAA1854, SLITL1; ORFNames=UNQ9197/PRO34756;
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 {ECO:0000312|EMBL:CAC18888.1};
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAC18888.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA   Redolfi E., Susani L., Mumm S., Stephan A., Reinbold R.A., Labella T.,
RA   Trent J.M., Vezzoni P., Zucchi T.;
RT   "The structural characterization of the new gene SLITL1 reveals the
RT   presence of an other novel gene embedded within SLITL1 first intron.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC03566.1};
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-566.
RC   TISSUE=Brain {ECO:0000312|EMBL:BAB47483.1};
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [7] {ECO:0000305}
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain {ECO:0000269|PubMed:14557068}, and
RC   Brain tumor {ECO:0000269|PubMed:14557068};
RX   PubMed=14557068; DOI=10.1016/s0378-1119(03)00715-7;
RA   Aruga J., Yokota N., Mikoshiba K.;
RT   "Human SLITRK family genes: genomic organization and expression profiling
RT   in normal brain and brain tumor tissue.";
RL   Gene 315:87-94(2003).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS MET-89;
RP   PHE-549 AND PRO-601.
RX   PubMed=27812321; DOI=10.3389/fnmol.2016.00104;
RA   Kang H., Han K.A., Won S.Y., Kim H.M., Lee Y.H., Ko J., Um J.W.;
RT   "Slitrk missense mutations associated with neuropsychiatric disorders
RT   distinctively impair Slitrk trafficking and synapse formation.";
RL   Front. Mol. Neurosci. 9:104-104(2016).
RN   [9]
RP   FUNCTION.
RX   PubMed=27273464; DOI=10.1038/srep27343;
RA   Beaubien F., Raja R., Kennedy T.E., Fournier A.E., Cloutier J.F.;
RT   "Slitrk1 is localized to excitatory synapses and promotes their
RT   development.";
RL   Sci. Rep. 6:27343-27343(2016).
RN   [10]
RP   VARIANTS MET-89 AND PHE-549.
RX   PubMed=20479760; DOI=10.1038/mp.2010.54;
RA   Piton A., Gauthier J., Hamdan F.F., Lafreniere R.G., Yang Y., Henrion E.,
RA   Laurent S., Noreau A., Thibodeau P., Karemera L., Spiegelman D., Kuku F.,
RA   Duguay J., Destroismaisons L., Jolivet P., Cote M., Lachapelle K.,
RA   Diallo O., Raymond A., Marineau C., Champagne N., Xiong L., Gaspar C.,
RA   Riviere J.B., Tarabeux J., Cossette P., Krebs M.O., Rapoport J.L.,
RA   Addington A., Delisi L.E., Mottron L., Joober R., Fombonne E., Drapeau P.,
RA   Rouleau G.A.;
RT   "Systematic resequencing of X-chromosome synaptic genes in autism spectrum
RT   disorder and schizophrenia.";
RL   Mol. Psychiatry 16:867-880(2011).
CC   -!- FUNCTION: It is involved in synaptogenesis and promotes excitatory
CC       synapse differentiation (PubMed:27273464, PubMed:27812321). Suppresses
CC       neurite outgrowth (By similarity). {ECO:0000250|UniProtKB:Q810C0,
CC       ECO:0000269|PubMed:27273464, ECO:0000269|PubMed:27812321}.
CC   -!- SUBUNIT: Interacts with PTPRD; this interaction is PTPRD splicing-
CC       dependent and may induce pre-synaptic differentiation.
CC       {ECO:0000250|UniProtKB:Q810C0}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cell membrane
CC       {ECO:0000269|PubMed:27812321}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000305};
CC         IsoId=Q9H156-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q9H156-2; Sequence=VSP_050706, VSP_050707;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the cerebral cortex of
CC       the brain but also at low levels in the spinal cord and medulla. Also
CC       expressed in some astrocytic brain tumors such as astrocytomas,
CC       oligodendrogliomas, glioblastomas, gangliogliomas and primitive
CC       neuroectodermal tumors. {ECO:0000269|PubMed:14557068}.
CC   -!- SIMILARITY: Belongs to the SLITRK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47483.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y19205; CAC80724.1; -; Genomic_DNA.
DR   EMBL; AY358828; AAQ89187.1; -; mRNA.
DR   EMBL; AK091015; BAC03566.1; -; mRNA.
DR   EMBL; AK289732; BAF82421.1; -; mRNA.
DR   EMBL; AL109653; CAI41645.1; -; Genomic_DNA.
DR   EMBL; AL109653; CAC18888.1; -; Genomic_DNA.
DR   EMBL; BC113011; AAI13012.1; -; mRNA.
DR   EMBL; BC113012; AAI13013.1; -; mRNA.
DR   EMBL; AB058757; BAB47483.1; ALT_INIT; mRNA.
DR   CCDS; CCDS14680.1; -. [Q9H156-1]
DR   RefSeq; NP_001137475.1; NM_001144003.2. [Q9H156-1]
DR   RefSeq; NP_001137476.1; NM_001144004.2. [Q9H156-1]
DR   RefSeq; NP_001137477.1; NM_001144005.2. [Q9H156-1]
DR   RefSeq; NP_001137478.1; NM_001144006.2. [Q9H156-1]
DR   RefSeq; NP_001137480.1; NM_001144008.2. [Q9H156-1]
DR   RefSeq; NP_001137481.1; NM_001144009.2. [Q9H156-1]
DR   RefSeq; NP_001137482.1; NM_001144010.2. [Q9H156-1]
DR   RefSeq; NP_115928.1; NM_032539.4. [Q9H156-1]
DR   RefSeq; XP_005262399.1; XM_005262342.3. [Q9H156-1]
DR   RefSeq; XP_005262400.1; XM_005262343.3. [Q9H156-1]
DR   RefSeq; XP_005262401.1; XM_005262344.3. [Q9H156-1]
DR   RefSeq; XP_005262402.1; XM_005262345.3. [Q9H156-1]
DR   AlphaFoldDB; Q9H156; -.
DR   SMR; Q9H156; -.
DR   BioGRID; 124160; 2.
DR   STRING; 9606.ENSP00000359521; -.
DR   GlyGen; Q9H156; 4 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9H156; -.
DR   PhosphoSitePlus; Q9H156; -.
DR   BioMuta; SLITRK2; -.
DR   DMDM; 46397026; -.
DR   jPOST; Q9H156; -.
DR   MassIVE; Q9H156; -.
DR   PaxDb; Q9H156; -.
DR   PeptideAtlas; Q9H156; -.
DR   PRIDE; Q9H156; -.
DR   ProteomicsDB; 80355; -. [Q9H156-1]
DR   ProteomicsDB; 80356; -. [Q9H156-2]
DR   Antibodypedia; 30574; 148 antibodies from 28 providers.
DR   DNASU; 84631; -.
DR   Ensembl; ENST00000335565.6; ENSP00000334374.5; ENSG00000185985.11. [Q9H156-1]
DR   Ensembl; ENST00000370490.1; ENSP00000359521.1; ENSG00000185985.11. [Q9H156-1]
DR   GeneID; 84631; -.
DR   KEGG; hsa:84631; -.
DR   MANE-Select; ENST00000335565.6; ENSP00000334374.5; NM_032539.5; NP_115928.1.
DR   UCSC; uc033eyj.2; human. [Q9H156-1]
DR   CTD; 84631; -.
DR   DisGeNET; 84631; -.
DR   GeneCards; SLITRK2; -.
DR   HGNC; HGNC:13449; SLITRK2.
DR   HPA; ENSG00000185985; Tissue enhanced (brain, retina).
DR   MIM; 300561; gene.
DR   neXtProt; NX_Q9H156; -.
DR   OpenTargets; ENSG00000185985; -.
DR   PharmGKB; PA134968225; -.
DR   VEuPathDB; HostDB:ENSG00000185985; -.
DR   eggNOG; ENOG502QR6C; Eukaryota.
DR   GeneTree; ENSGT00940000161248; -.
DR   InParanoid; Q9H156; -.
DR   OMA; GEQVAYY; -.
DR   OrthoDB; 217854at2759; -.
DR   PhylomeDB; Q9H156; -.
DR   TreeFam; TF351826; -.
DR   PathwayCommons; Q9H156; -.
DR   Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR   BioGRID-ORCS; 84631; 10 hits in 697 CRISPR screens.
DR   ChiTaRS; SLITRK2; human.
DR   GeneWiki; SLITRK2; -.
DR   GenomeRNAi; 84631; -.
DR   Pharos; Q9H156; Tbio.
DR   PRO; PR:Q9H156; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9H156; protein.
DR   Bgee; ENSG00000185985; Expressed in ventricular zone and 124 other tissues.
DR   ExpressionAtlas; Q9H156; baseline and differential.
DR   Genevisible; Q9H156; HS.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR   GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
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; IPR000372; LRRNT.
DR   InterPro; IPR043326; Slitrk.
DR   PANTHER; PTHR45773; PTHR45773; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 10.
DR   SMART; SM00082; LRRCT; 2.
DR   SMART; SM00013; LRRNT; 2.
DR   PROSITE; PS51450; LRR; 12.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..845
FT                   /note="SLIT and NTRK-like protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032675"
FT   TOPO_DOM        22..621
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        622..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        643..845
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          63..84
FT                   /note="LRR 1"
FT   REPEAT          87..108
FT                   /note="LRR 2"
FT   REPEAT          111..132
FT                   /note="LRR 3"
FT   REPEAT          135..156
FT                   /note="LRR 4"
FT   REPEAT          159..180
FT                   /note="LRR 5"
FT   REPEAT          182..203
FT                   /note="LRR 6"
FT   DOMAIN          216..265
FT                   /note="LRRCT 1"
FT   DOMAIN          331..373
FT                   /note="LRRNT"
FT   REPEAT          376..397
FT                   /note="LRR 7"
FT   REPEAT          400..421
FT                   /note="LRR 8"
FT   REPEAT          424..445
FT                   /note="LRR 9"
FT   REPEAT          448..469
FT                   /note="LRR 10"
FT   REPEAT          472..493
FT                   /note="LRR 11"
FT   REPEAT          495..516
FT                   /note="LRR 12"
FT   DOMAIN          529..580
FT                   /note="LRRCT 2"
FT   REGION          167..215
FT                   /note="Required for interaction with PTPRD"
FT                   /evidence="ECO:0000250|UniProtKB:Q810C0"
FT   REGION          263..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         756
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q810C0"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..35
FT                   /evidence="ECO:0000250|UniProtKB:Q810C0"
FT   DISULFID        33..46
FT                   /evidence="ECO:0000250|UniProtKB:Q810C0"
FT   DISULFID        220..243
FT                   /evidence="ECO:0000250|UniProtKB:Q810C0"
FT   DISULFID        222..263
FT                   /evidence="ECO:0000250|UniProtKB:Q810C0"
FT   VAR_SEQ         719..733
FT                   /note="SYSNLEEKKEEPATP -> KTSLENIWRPCLHKK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_050706"
FT   VAR_SEQ         734..845
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_050707"
FT   VARIANT         89
FT                   /note="V -> M (found in a patient with schizophrenia;
FT                   unknown pathological significance; does not impair
FT                   synaptogenesis; no effect on localization to cell membrane;
FT                   dbSNP:rs1402893590)"
FT                   /evidence="ECO:0000269|PubMed:20479760,
FT                   ECO:0000269|PubMed:27812321"
FT                   /id="VAR_077630"
FT   VARIANT         549
FT                   /note="S -> F (found in a patient with schizophrenia;
FT                   unknown pathological significance; does not impair
FT                   synaptogenesis; no effect on localization to cell membrane;
FT                   dbSNP:rs1239180055)"
FT                   /evidence="ECO:0000269|PubMed:20479760,
FT                   ECO:0000269|PubMed:27812321"
FT                   /id="VAR_077631"
FT   VARIANT         601
FT                   /note="S -> P (does not affect synaptogenesis; no effect on
FT                   localization to cell membrane; dbSNP:rs2295336)"
FT                   /evidence="ECO:0000269|PubMed:27812321"
FT                   /id="VAR_027756"
FT   CONFLICT        721
FT                   /note="S -> G (in Ref. 3; BAC03566)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   845 AA;  95404 MW;  20E35DBD1584F9A4 CRC64;
     MLSGVWFLSV LTVAGILQTE SRKTAKDICK IRCLCEEKEN VLNINCENKG FTTVSLLQPP
     QYRIYQLFLN GNLLTRLYPN EFVNYSNAVT LHLGNNGLQE IRTGAFSGLK TLKRLHLNNN
     KLEILREDTF LGLESLEYLQ ADYNYISAIE AGAFSKLNKL KVLILNDNLL LSLPSNVFRF
     VLLTHLDLRG NRLKVMPFAG VLEHIGGIME IQLEENPWNC TCDLLPLKAW LDTITVFVGE
     IVCETPFRLH GKDVTQLTRQ DLCPRKSASD SSQRGSHADT HVQRLSPTMN PALNPTRAPK
     ASRPPKMRNR PTPRVTVSKD RQSFGPIMVY QTKSPVPLTC PSSCVCTSQS SDNGLNVNCQ
     ERKFTNISDL QPKPTSPKKL YLTGNYLQTV YKNDLLEYSS LDLLHLGNNR IAVIQEGAFT
     NLTSLRRLYL NGNYLEVLYP SMFDGLQSLQ YLYLEYNVIK EIKPLTFDAL INLQLLFLNN
     NLLRSLPDNI FGGTALTRLN LRNNHFSHLP VKGVLDQLPA FIQIDLQENP WDCTCDIMGL
     KDWTEHANSP VIINEVTCES PAKHAGEILK FLGREAICPD SPNLSDGTVL SMNHNTDTPR
     SLSVSPSSYP ELHTEVPLSV LILGLLVVFI LSVCFGAGLF VFVLKRRKGV PSVPRNTNNL
     DVSSFQLQYG SYNTETHDKT DGHVYNYIPP PVGQMCQNPI YMQKEGDPVA YYRNLQEFSY
     SNLEEKKEEP ATPAYTISAT ELLEKQATPR EPELLYQNIA ERVKELPSAG LVHYNFCTLP
     KRQFAPSYES RRQNQDRINK TVLYGTPRKC FVGQSKPNHP LLQAKPQSEP DYLEVLEKQT
     AISQL
 
 
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