ROBO1_HUMAN
ID ROBO1_HUMAN Reviewed; 1651 AA.
AC Q9Y6N7; B2RXI1; D3DU36; E9PD49; Q1RMC7; Q7Z300; Q9BUS7;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Roundabout homolog 1;
DE AltName: Full=Deleted in U twenty twenty;
DE AltName: Full=H-Robo-1;
DE Flags: Precursor;
GN Name=ROBO1; Synonyms=DUTT1;
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 [MRNA] (ISOFORM 1).
RX PubMed=9458045; DOI=10.1016/s0092-8674(00)80915-0;
RA Kidd T., Brose K., Mitchell K.J., Fetter R.D., Tessier-Lavigne M.,
RA Goodman C.S., Tear G.;
RT "Roundabout controls axon crossing of the CNS midline and defines a novel
RT subfamily of evolutionarily conserved guidance receptors.";
RL Cell 92:205-215(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1158-1651 (ISOFORMS 1/2/3/4).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1651 (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH SLIT2.
RC TISSUE=Fetal brain;
RX PubMed=10102268; DOI=10.1016/s0092-8674(00)80590-5;
RA Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
RA Tessier-Lavigne M., Kidd T.;
RT "Slit proteins bind Robo receptors and have an evolutionarily conserved
RT role in repulsive axon guidance.";
RL Cell 96:795-806(1999).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9608531; DOI=10.1006/mcne.1998.0672;
RA Sundaresan V., Roberts I., Bateman A., Bankier A., Sheppard M., Hobbs C.,
RA Xiong J., Minna J., Latif F., Lerman M., Rabbitts P.;
RT "The DUTT1 gene, a novel NCAM family member is expressed in developing
RT murine neural tissues and has an unusually broad pattern of expression.";
RL Mol. Cell. Neurosci. 11:29-35(1998).
RN [8]
RP MAPPING, AND IDENTIFICATION (ISOFORM 3).
RX PubMed=9796701; DOI=10.1038/sj.onc.1202103;
RA Sundaresan V., Chung G., Heppell-Parton A., Xiong J., Grundy C.,
RA Roberts I., James L., Cahn A., Bench A., Douglas J., Minna J., Sekido Y.,
RA Lerman M., Latif F., Bergh J., Li H., Lowe N., Ogilvie D., Rabbitts P.;
RT "Homozygous deletions at 3p12 in breast and lung cancer.";
RL Oncogene 17:1723-1729(1998).
RN [9]
RP PHOSPHORYLATION AT TYR-1038; TYR-1073 AND TYR-1114.
RX PubMed=10892742; DOI=10.1016/s0092-8674(00)80883-1;
RA Bashaw G.J., Kidd T., Murray D., Pawson T., Goodman C.S.;
RT "Repulsive axon guidance: Abelson and Enabled play opposing roles
RT downstream of the roundabout receptor.";
RL Cell 101:703-715(2000).
RN [10]
RP INTERACTION WITH SLIT2.
RX PubMed=11404413; DOI=10.1523/jneurosci.21-12-04281.2001;
RA Nguyen-Ba-Charvet K.T., Brose K., Ma L., Wang K.H., Marillat V., Sotelo C.,
RA Tessier-Lavigne M., Chedotal A.;
RT "Diversity and specificity of actions of Slit2 proteolytic fragments in
RT axon guidance.";
RL J. Neurosci. 21:4281-4289(2001).
RN [11]
RP PROMOTER HYPERMETHYLATION, AND VARIANTS ASN-1055 AND ASP-1533.
RX PubMed=12082532; DOI=10.1038/sj.onc.1205421;
RA Dallol A., Forgacs E., Martinez A., Sekido Y., Walker R., Kishida T.,
RA Rabbitts P., Maher E.R., Minna J.D., Latif F.;
RT "Tumour specific promoter region methylation of the human homologue of the
RT Drosophila Roundabout gene DUTT1 (ROBO1) in human cancers.";
RL Oncogene 21:3020-3028(2002).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940; SER-1055; THR-1240 AND
RP SER-1297, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940; THR-948 AND SER-1055,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP SUBUNIT.
RX PubMed=24673457; DOI=10.1042/bj20140190;
RA Zakrys L., Ward R.J., Pediani J.D., Godin A.G., Graham G.J., Milligan G.;
RT "Roundabout 1 exists predominantly as a basal dimeric complex and this is
RT unaffected by binding of the ligand Slit2.";
RL Biochem. J. 461:61-73(2014).
RN [18]
RP INTERACTION WITH FLRT3, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24560577; DOI=10.1016/j.cub.2014.01.042;
RA Leyva-Diaz E., del Toro D., Menal M.J., Cambray S., Susin R.,
RA Tessier-Lavigne M., Klein R., Egea J., Lopez-Bendito G.;
RT "FLRT3 is a Robo1-interacting protein that determines Netrin-1 attraction
RT in developing axons.";
RL Curr. Biol. 24:494-508(2014).
RN [19]
RP FUNCTION, AND INTERACTION WITH MYO9B.
RX PubMed=26529257; DOI=10.1172/jci81673;
RA Kong R., Yi F., Wen P., Liu J., Chen X., Ren J., Li X., Shang Y., Nie Y.,
RA Wu K., Fan D., Zhu L., Feng W., Wu J.Y.;
RT "Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression.";
RL J. Clin. Invest. 125:4407-4420(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 61-166 IN COMPLEX WITH SLIT2,
RP INTERACTION WITH SLIT2, AND DISULFIDE BONDS.
RX PubMed=17848514; DOI=10.1073/pnas.0705310104;
RA Morlot C., Thielens N.M., Ravelli R.B., Hemrika W., Romijn R.A., Gros P.,
RA Cusack S., McCarthy A.A.;
RT "Structural insights into the Slit-Robo complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14923-14928(2007).
RN [21]
RP STRUCTURE BY NMR OF 454-564, AND DISULFIDE BOND.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fifth Ig-like domain from human roundabout
RT homolog 1.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses
CC to molecular guidance cues in cellular migration, including axonal
CC navigation at the ventral midline of the neural tube and projection of
CC axons to different regions during neuronal development
CC (PubMed:10102268, PubMed:24560577). Interaction with the intracellular
CC domain of FLRT3 mediates axon attraction towards cells expressing NTN1
CC (PubMed:24560577). In axon growth cones, the silencing of the
CC attractive effect of NTN1 by SLIT2 may require the formation of a
CC ROBO1-DCC complex (By similarity). Plays a role in the regulation of
CC cell migration via its interaction with MYO9B; inhibits MYO9B-mediated
CC stimulation of RHOA GTPase activity, and thereby leads to increased
CC levels of active, GTP-bound RHOA (PubMed:26529257). May be required for
CC lung development (By similarity). {ECO:0000250|UniProtKB:O89026,
CC ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:24560577,
CC ECO:0000269|PubMed:26529257, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. Dimerization is mediated by the extracellular
CC domain and is independent of SLIT liganding (PubMed:24673457).
CC Interacts with SLIT1 (By similarity). Interacts with SLIT2
CC (PubMed:10102268, PubMed:11404413, PubMed:17848514). Interacts with
CC FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-GAP domain)
CC (PubMed:26529257). {ECO:0000250|UniProtKB:O89026,
CC ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:11404413,
CC ECO:0000269|PubMed:17848514, ECO:0000269|PubMed:24560577,
CC ECO:0000269|PubMed:24673457, ECO:0000269|PubMed:26529257}.
CC -!- INTERACTION:
CC Q9Y6N7; O94813: SLIT2; NbExp=2; IntAct=EBI-399762, EBI-1236865;
CC Q9Y6N7; O75044: SRGAP2; NbExp=3; IntAct=EBI-399762, EBI-1051034;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24560577};
CC Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC axon {ECO:0000250|UniProtKB:O89026}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:O55005};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:O55005}.
CC Note=Detected at growth cones in thalamus neurons. Detected at growth
CC cones in thalamus neurons (By similarity). PRRG4 prevents cell surface
CC location and both colocalize in the Endoplasmic reticulum/Golgi
CC adjacent to the cell nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O55005, ECO:0000250|UniProtKB:O89026}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9Y6N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6N7-2; Sequence=VSP_010646;
CC Name=3;
CC IsoId=Q9Y6N7-3; Sequence=VSP_010643, VSP_010644, VSP_010645;
CC Name=4;
CC IsoId=Q9Y6N7-4; Sequence=VSP_010643, VSP_010644;
CC Name=5;
CC IsoId=Q9Y6N7-5; Sequence=VSP_043881, VSP_010645, VSP_043882;
CC Name=6;
CC IsoId=Q9Y6N7-6; Sequence=VSP_043881, VSP_010645, VSP_043882,
CC VSP_046084;
CC -!- TISSUE SPECIFICITY: Widely expressed, with exception of kidney.
CC {ECO:0000269|PubMed:9608531}.
CC -!- PTM: Ubiquitinated. May be deubiquitinated by USP33.
CC {ECO:0000250|UniProtKB:O89026}.
CC -!- MISCELLANEOUS: Maps within a region of overlapping homozygous deletions
CC characterized in both small cell lung cancer cell lines (SCLC) and in a
CC breast cancer cell line. The promoter region of ROBO1 shows complete
CC hypermethylation of CpG sites in the BT-20 breast tumor cell lines,
CC some primary invasive breast carcinomasa and some primary clear cell
CC renal cell carcinomas (CC-RCC).
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ROBO1ID42140ch3p12.html";
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DR EMBL; AF040990; AAC39575.1; -; mRNA.
DR EMBL; Z95705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC055731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471110; EAW68884.1; -; Genomic_DNA.
DR EMBL; CH471110; EAW68885.1; -; Genomic_DNA.
DR EMBL; BC001969; AAH01969.1; -; mRNA.
DR EMBL; BC115022; AAI15023.1; -; mRNA.
DR EMBL; BC157861; AAI57862.1; -; mRNA.
DR EMBL; BC171855; AAI71855.1; -; mRNA.
DR EMBL; BX538319; CAD98093.1; -; mRNA.
DR CCDS; CCDS46872.2; -. [Q9Y6N7-5]
DR CCDS; CCDS54610.1; -. [Q9Y6N7-6]
DR CCDS; CCDS54611.1; -. [Q9Y6N7-1]
DR RefSeq; NP_001139317.1; NM_001145845.1. [Q9Y6N7-6]
DR RefSeq; NP_002932.1; NM_002941.3. [Q9Y6N7-1]
DR RefSeq; NP_598334.2; NM_133631.3. [Q9Y6N7-5]
DR RefSeq; XP_006713340.1; XM_006713277.2. [Q9Y6N7-3]
DR RefSeq; XP_016862472.1; XM_017006983.1. [Q9Y6N7-4]
DR PDB; 2EO9; NMR; -; A=454-564.
DR PDB; 2V9Q; X-ray; 2.50 A; A=61-266.
DR PDB; 2V9R; X-ray; 2.00 A; A=61-266.
DR PDB; 2V9T; X-ray; 1.70 A; A=61-166.
DR PDB; 3WIH; X-ray; 1.70 A; A/B=777-873.
DR PDB; 4HLJ; X-ray; 1.80 A; A=660-897.
DR PDB; 5O5G; X-ray; 3.03 A; A=63-446.
DR PDB; 5O5I; X-ray; 3.01 A; A=454-543.
DR PDB; 5OPE; X-ray; 2.54 A; A=63-447.
DR PDB; 6A77; X-ray; 2.00 A; A=455-543.
DR PDB; 6A78; X-ray; 2.10 A; A/B=455-543.
DR PDB; 6A79; X-ray; 2.31 A; A/B=455-543.
DR PDBsum; 2EO9; -.
DR PDBsum; 2V9Q; -.
DR PDBsum; 2V9R; -.
DR PDBsum; 2V9T; -.
DR PDBsum; 3WIH; -.
DR PDBsum; 4HLJ; -.
DR PDBsum; 5O5G; -.
DR PDBsum; 5O5I; -.
DR PDBsum; 5OPE; -.
DR PDBsum; 6A77; -.
DR PDBsum; 6A78; -.
DR PDBsum; 6A79; -.
DR AlphaFoldDB; Q9Y6N7; -.
DR SMR; Q9Y6N7; -.
DR BioGRID; 112018; 69.
DR DIP; DIP-33034N; -.
DR ELM; Q9Y6N7; -.
DR IntAct; Q9Y6N7; 24.
DR MINT; Q9Y6N7; -.
DR STRING; 9606.ENSP00000420321; -.
DR GlyGen; Q9Y6N7; 7 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9Y6N7; -.
DR PhosphoSitePlus; Q9Y6N7; -.
DR SwissPalm; Q9Y6N7; -.
DR BioMuta; ROBO1; -.
DR DMDM; 49036500; -.
DR EPD; Q9Y6N7; -.
DR jPOST; Q9Y6N7; -.
DR MassIVE; Q9Y6N7; -.
DR MaxQB; Q9Y6N7; -.
DR PaxDb; Q9Y6N7; -.
DR PeptideAtlas; Q9Y6N7; -.
DR PRIDE; Q9Y6N7; -.
DR ProteomicsDB; 19585; -.
DR ProteomicsDB; 86744; -. [Q9Y6N7-1]
DR ProteomicsDB; 86745; -. [Q9Y6N7-2]
DR ProteomicsDB; 86746; -. [Q9Y6N7-3]
DR ProteomicsDB; 86747; -. [Q9Y6N7-4]
DR ProteomicsDB; 86748; -. [Q9Y6N7-5]
DR ABCD; Q9Y6N7; 3 sequenced antibodies.
DR Antibodypedia; 4617; 368 antibodies from 44 providers.
DR DNASU; 6091; -.
DR Ensembl; ENST00000464233.6; ENSP00000420321.1; ENSG00000169855.21. [Q9Y6N7-1]
DR Ensembl; ENST00000467549.5; ENSP00000417992.1; ENSG00000169855.21. [Q9Y6N7-6]
DR Ensembl; ENST00000495273.5; ENSP00000420637.1; ENSG00000169855.21. [Q9Y6N7-5]
DR GeneID; 6091; -.
DR KEGG; hsa:6091; -.
DR MANE-Select; ENST00000464233.6; ENSP00000420321.1; NM_002941.4; NP_002932.1.
DR UCSC; uc003dqc.3; human. [Q9Y6N7-1]
DR CTD; 6091; -.
DR DisGeNET; 6091; -.
DR GeneCards; ROBO1; -.
DR HGNC; HGNC:10249; ROBO1.
DR HPA; ENSG00000169855; Low tissue specificity.
DR MalaCards; ROBO1; -.
DR MIM; 602430; gene.
DR neXtProt; NX_Q9Y6N7; -.
DR OpenTargets; ENSG00000169855; -.
DR Orphanet; 95496; Pituitary stalk interruption syndrome.
DR PharmGKB; PA34620; -.
DR VEuPathDB; HostDB:ENSG00000169855; -.
DR eggNOG; KOG4222; Eukaryota.
DR GeneTree; ENSGT00940000154477; -.
DR HOGENOM; CLU_003227_3_0_1; -.
DR InParanoid; Q9Y6N7; -.
DR OMA; SHNDCSI; -.
DR OrthoDB; 45439at2759; -.
DR PhylomeDB; Q9Y6N7; -.
DR TreeFam; TF351053; -.
DR PathwayCommons; Q9Y6N7; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-376176; Signaling by ROBO receptors.
DR Reactome; R-HSA-428540; Activation of RAC1.
DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
DR Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-HSA-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-HSA-8985801; Regulation of cortical dendrite branching.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR SignaLink; Q9Y6N7; -.
DR SIGNOR; Q9Y6N7; -.
DR BioGRID-ORCS; 6091; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; ROBO1; human.
DR EvolutionaryTrace; Q9Y6N7; -.
DR GeneWiki; ROBO1; -.
DR GenomeRNAi; 6091; -.
DR Pharos; Q9Y6N7; Tbio.
DR PRO; PR:Q9Y6N7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6N7; protein.
DR Bgee; ENSG00000169855; Expressed in ventricular zone and 206 other tissues.
DR ExpressionAtlas; Q9Y6N7; baseline and differential.
DR Genevisible; Q9Y6N7; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008046; F:axon guidance receptor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0035904; P:aorta development; ISS:BHF-UCL.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; IDA:UniProtKB.
DR GO; GO:0003272; P:endocardial cushion formation; ISS:BHF-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0050925; P:negative regulation of negative chemotaxis; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:BHF-UCL.
DR GO; GO:0035481; P:positive regulation of Notch signaling pathway involved in heart induction; ISS:BHF-UCL.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0035385; P:Roundabout signaling pathway; IMP:UniProtKB.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 8.
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 InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR032986; Robo1.
DR PANTHER; PTHR12231:SF243; PTHR12231:SF243; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Chemotaxis; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1651
FT /note="Roundabout homolog 1"
FT /id="PRO_0000031033"
FT TOPO_DOM 26..897
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 919..1651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 68..164
FT /note="Ig-like C2-type 1"
FT DOMAIN 170..257
FT /note="Ig-like C2-type 2"
FT DOMAIN 262..346
FT /note="Ig-like C2-type 3"
FT DOMAIN 351..446
FT /note="Ig-like C2-type 4"
FT DOMAIN 455..541
FT /note="Ig-like C2-type 5"
FT DOMAIN 563..657
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 676..773
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 778..874
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1038
FT /note="Phosphotyrosine; by ABL; in vitro"
FT /evidence="ECO:0000269|PubMed:10892742"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1073
FT /note="Phosphotyrosine; by ABL; in vitro"
FT /evidence="ECO:0000269|PubMed:10892742"
FT MOD_RES 1114
FT /note="Phosphotyrosine; by ABL; in vitro"
FT /evidence="ECO:0000269|PubMed:10892742"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17848514, ECO:0007744|PDB:2V9Q,
FT ECO:0007744|PDB:2V9R, ECO:0007744|PDB:2V9T"
FT DISULFID 191..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17848514, ECO:0007744|PDB:2V9Q,
FT ECO:0007744|PDB:2V9R"
FT DISULFID 283..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 372..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 476..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|Ref.21, ECO:0007744|PDB:2EO9"
FT VAR_SEQ 1..57
FT /note="MKWKHVPFLVMISLLSLSPNHLFLAQLIPDPEDVERGNDHGTPIPTSDNDDN
FT SLGYT -> MIAEPAHFYLFGLICLCS (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043881"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010643"
FT VAR_SEQ 40..57
FT /note="HGTPIPTSDNDDNSLGYT -> MIAEPAHFYLFGLICLCS (in isoform
FT 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010644"
FT VAR_SEQ 348
FT /note="Q -> QVGS (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010645"
FT VAR_SEQ 543
FT /note="Q -> QGKVN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010646"
FT VAR_SEQ 938..946
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043882"
FT VAR_SEQ 1013..1067
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046084"
FT VARIANT 336
FT /note="V -> A (in dbSNP:rs9647397)"
FT /id="VAR_053640"
FT VARIANT 1055
FT /note="S -> N (in a breast cancer sample;
FT dbSNP:rs919603543)"
FT /evidence="ECO:0000269|PubMed:12082532"
FT /id="VAR_019071"
FT VARIANT 1091
FT /note="S -> N (in dbSNP:rs35456279)"
FT /id="VAR_053641"
FT VARIANT 1533
FT /note="E -> D (in a breast cancer sample;
FT dbSNP:rs36055689)"
FT /evidence="ECO:0000269|PubMed:12082532"
FT /id="VAR_019072"
FT CONFLICT 182
FT /note="A -> V (in Ref. 4; AAI15023)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="F -> L (in Ref. 4; AAI15023)"
FT /evidence="ECO:0000305"
FT CONFLICT 1095
FT /note="G -> S (in Ref. 5; CAD98093)"
FT /evidence="ECO:0000305"
FT CONFLICT 1223
FT /note="M -> T (in Ref. 2; Z95705)"
FT /evidence="ECO:0000305"
FT CONFLICT 1443
FT /note="P -> L (in Ref. 5; CAD98093)"
FT /evidence="ECO:0000305"
FT CONFLICT 1536
FT /note="D -> G (in Ref. 2; Z95705)"
FT /evidence="ECO:0000305"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2V9T"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2V9T"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:5O5G"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:2V9Q"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:2V9R"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2V9R"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2V9R"
FT HELIX 261..266
FT /evidence="ECO:0007829|PDB:2V9Q"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5OPE"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 338..355
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:5OPE"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 436..446
FT /evidence="ECO:0007829|PDB:5OPE"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:6A77"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:6A78"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:6A77"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 521..529
FT /evidence="ECO:0007829|PDB:6A77"
FT STRAND 532..543
FT /evidence="ECO:0007829|PDB:6A77"
FT HELIX 666..675
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 691..699
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 706..715
FT /evidence="ECO:0007829|PDB:4HLJ"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 724..728
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 735..738
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 746..755
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 780..786
FT /evidence="ECO:0007829|PDB:3WIH"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:3WIH"
FT STRAND 794..799
FT /evidence="ECO:0007829|PDB:3WIH"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:4HLJ"
FT STRAND 812..818
FT /evidence="ECO:0007829|PDB:3WIH"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:3WIH"
FT STRAND 826..831
FT /evidence="ECO:0007829|PDB:3WIH"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:3WIH"
FT STRAND 848..854
FT /evidence="ECO:0007829|PDB:3WIH"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:3WIH"
FT HELIX 880..883
FT /evidence="ECO:0007829|PDB:4HLJ"
SQ SEQUENCE 1651 AA; 180930 MW; 9D98CD7CAB73074D CRC64;
MKWKHVPFLV MISLLSLSPN HLFLAQLIPD PEDVERGNDH GTPIPTSDND DNSLGYTGSR
LRQEDFPPRI VEHPSDLIVS KGEPATLNCK AEGRPTPTIE WYKGGERVET DKDDPRSHRM
LLPSGSLFFL RIVHGRKSRP DEGVYVCVAR NYLGEAVSHN ASLEVAILRD DFRQNPSDVM
VAVGEPAVME CQPPRGHPEP TISWKKDGSP LDDKDERITI RGGKLMITYT RKSDAGKYVC
VGTNMVGERE SEVAELTVLE RPSFVKRPSN LAVTVDDSAE FKCEARGDPV PTVRWRKDDG
ELPKSRYEIR DDHTLKIRKV TAGDMGSYTC VAENMVGKAE ASATLTVQEP PHFVVKPRDQ
VVALGRTVTF QCEATGNPQP AIFWRREGSQ NLLFSYQPPQ SSSRFSVSQT GDLTITNVQR
SDVGYYICQT LNVAGSIITK AYLEVTDVIA DRPPPVIRQG PVNQTVAVDG TFVLSCVATG
SPVPTILWRK DGVLVSTQDS RIKQLENGVL QIRYAKLGDT GRYTCIASTP SGEATWSAYI
EVQEFGVPVQ PPRPTDPNLI PSAPSKPEVT DVSRNTVTLS WQPNLNSGAT PTSYIIEAFS
HASGSSWQTV AENVKTETSA IKGLKPNAIY LFLVRAANAY GISDPSQISD PVKTQDVLPT
SQGVDHKQVQ RELGNAVLHL HNPTVLSSSS IEVHWTVDQQ SQYIQGYKIL YRPSGANHGE
SDWLVFEVRT PAKNSVVIPD LRKGVNYEIK ARPFFNEFQG ADSEIKFAKT LEEAPSAPPQ
GVTVSKNDGN GTAILVSWQP PPEDTQNGMV QEYKVWCLGN ETRYHINKTV DGSTFSVVIP
FLVPGIRYSV EVAASTGAGS GVKSEPQFIQ LDAHGNPVSP EDQVSLAQQI SDVVKQPAFI
AGIGAACWII LMVFSIWLYR HRKKRNGLTS TYAGIRKVPS FTFTPTVTYQ RGGEAVSSGG
RPGLLNISEP AAQPWLADTW PNTGNNHNDC SISCCTAGNG NSDSNLTTYS RPADCIANYN
NQLDNKQTNL MLPESTVYGD VDLSNKINEM KTFNSPNLKD GRFVNPSGQP TPYATTQLIQ
SNLSNNMNNG SGDSGEKHWK PLGQQKQEVA PVQYNIVEQN KLNKDYRAND TVPPTIPYNQ
SYDQNTGGSY NSSDRGSSTS GSQGHKKGAR TPKVPKQGGM NWADLLPPPP AHPPPHSNSE
EYNISVDESY DQEMPCPVPP ARMYLQQDEL EEEEDERGPT PPVRGAASSP AAVSYSHQST
ATLTPSPQEE LQPMLQDCPE ETGHMQHQPD RRRQPVSPPP PPRPISPPHT YGYISGPLVS
DMDTDAPEEE EDEADMEVAK MQTRRLLLRG LEQTPASSVG DLESSVTGSM INGWGSASEE
DNISSGRSSV SSSDGSFFTD ADFAQAVAAA AEYAGLKVAR RQMQDAAGRR HFHASQCPRP
TSPVSTDSNM SAAVMQKTRP AKKLKHQPGH LRRETYTDDL PPPPVPPPAI KSPTAQSKTQ
LEVRPVVVPK LPSMDARTDR SSDRKGSSYK GREVLDGRQV VDMRTNPGDP REAQEQQNDG
KGRGNKAAKR DLPPAKTHLI QEDILPYCRP TFPTSNNPRD PSSSSSMSSR GSGSRQREQA
NVGRRNIAEM QVLGGYERGE DNNEELEETE S
