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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
 
 
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