ID ROBO2_HUMAN Reviewed; 1378 AA. AC Q9HCK4; O43608; Q19AB4; Q19AB5; DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=Roundabout homolog 2; DE Flags: Precursor; GN Name=ROBO2; Synonyms=KIAA1568; 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), AND ALTERNATIVE SPLICING. RX PubMed=16829019; DOI=10.1016/j.ygeno.2006.05.011; RA Yue Y., Grossmann B., Galetzka D., Zechner U., Haaf T.; RT "Isolation and differential expression of two isoforms of the ROBO2/Robo2 RT axon guidance receptor gene in humans and mice."; RL Genomics 88:772-778(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Yue Y., Grossmann B., Galetzka D., Zechner U., Haaf T.; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 845-1378 (ISOFORM 2). RC TISSUE=Ovary; 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] RP NUCLEOTIDE SEQUENCE [MRNA] OF 323-607. 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 [7] RP INTERACTION WITH SLIT2. 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 [8] 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 [9] RP STRUCTURE BY NMR OF 417-734. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fifth Ig-like domain and of first and second RT fibronectin type III domain from human roundabout homolog 2."; RL Submitted (AUG-2007) to the PDB data bank. RN [10] RP VARIANTS VUR2 THR-945 AND THR-1236, AND CHROMOSOMAL TRANSLOCATION WITH RP PCDH11Y. RX PubMed=17357069; DOI=10.1086/512735; RA Lu W., van Eerde A.M., Fan X., Quintero-Rivera F., Kulkarni S., RA Ferguson H., Kim H.-G., Fan Y., Xi Q., Li Q.-G., Sanlaville D., Andrews W., RA Sundaresan V., Bi W., Yan J., Giltay J.C., Wijmenga C., de Jong T.P.V.M., RA Feather S.A., Woolf A.S., Rao Y., Lupski J.R., Eccles M.R., Quade B.J., RA Gusella J.F., Morton C.C., Maas R.L.; RT "Disruption of ROBO2 is associated with urinary tract anomalies and confers RT risk of vesicoureteral reflux."; RL Am. J. Hum. Genet. 80:616-632(2007). CC -!- FUNCTION: Receptor for SLIT2, and probably SLIT1, which are thought to CC act as molecular guidance cue 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 -!- SUBUNIT: Interacts with SLIT2. {ECO:0000269|PubMed:10102268, CC ECO:0000269|PubMed:11404413}. CC -!- INTERACTION: CC Q9HCK4; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-399800, EBI-13345167; CC Q9HCK4; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-399800, EBI-10982110; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9HCK4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9HCK4-2; Sequence=VSP_010647; CC Name=3; CC IsoId=Q9HCK4-3; Sequence=VSP_043394; CC -!- DISEASE: Vesicoureteral reflux 2 (VUR2) [MIM:610878]: A disease CC belonging to the group of congenital anomalies of the kidney and CC urinary tract. It is characterized by the reflux of urine from the CC bladder into the ureters and sometimes into the kidneys, and is a risk CC factor for urinary tract infections. Primary disease results from a CC developmental defect of the ureterovesical junction. In combination CC with intrarenal reflux, the resulting inflammatory reaction may result CC in renal injury or scarring, also called reflux nephropathy. Extensive CC renal scarring impairs renal function and may predispose patients to CC hypertension, proteinuria, renal insufficiency and end-stage renal CC disease. {ECO:0000269|PubMed:17357069}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving ROBO2 is a cause of CC multiple congenital abnormalities, including severe bilateral VUR with CC ureterovesical junction defects. Translocation t(Y;3)(p11;p12) with CC PCDH11Y. This translocation disrupts ROBO2 and produces dominant- CC negative ROBO2 proteins that abrogate SLIT-ROBO signaling in vitro. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC39576.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB13394.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ533874; ABF83431.1; -; mRNA. DR EMBL; AB046788; BAB13394.1; ALT_INIT; mRNA. DR EMBL; DQ533873; ABF83430.1; -; mRNA. DR EMBL; AC016942; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC016952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC024256; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC067717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117514; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117515; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117516; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC126467; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC130004; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131005; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131154; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133040; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138974; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC064374; AAH64374.1; -; mRNA. DR EMBL; BC146772; AAI46773.1; -; mRNA. DR EMBL; AF040991; AAC39576.1; ALT_FRAME; mRNA. DR CCDS; CCDS43109.1; -. [Q9HCK4-1] DR CCDS; CCDS54609.1; -. [Q9HCK4-3] DR RefSeq; NP_001122401.1; NM_001128929.3. [Q9HCK4-3] DR RefSeq; NP_001276968.1; NM_001290039.1. DR RefSeq; NP_001276969.1; NM_001290040.1. DR RefSeq; NP_001276994.1; NM_001290065.1. DR RefSeq; NP_002933.1; NM_002942.4. [Q9HCK4-1] DR PDB; 1UEM; NMR; -; A=514-617. DR PDB; 1UJT; NMR; -; A=628-734. DR PDB; 2EDJ; NMR; -; A=417-509. DR PDB; 5NOI; X-ray; 2.40 A; A=311-509. DR PDB; 6I9S; X-ray; 2.48 A; A/B=126-312. DR PDB; 6IAA; X-ray; 3.60 A; A/B/C=22-859. DR PDBsum; 1UEM; -. DR PDBsum; 1UJT; -. DR PDBsum; 2EDJ; -. DR PDBsum; 5NOI; -. DR PDBsum; 6I9S; -. DR PDBsum; 6IAA; -. DR AlphaFoldDB; Q9HCK4; -. DR SMR; Q9HCK4; -. DR BioGRID; 112019; 37. DR IntAct; Q9HCK4; 32. DR MINT; Q9HCK4; -. DR STRING; 9606.ENSP00000417335; -. DR GlyCosmos; Q9HCK4; 6 sites, No reported glycans. DR GlyGen; Q9HCK4; 6 sites. DR iPTMnet; Q9HCK4; -. DR PhosphoSitePlus; Q9HCK4; -. DR BioMuta; ROBO2; -. DR DMDM; 49036496; -. DR EPD; Q9HCK4; -. DR jPOST; Q9HCK4; -. DR MassIVE; Q9HCK4; -. DR MaxQB; Q9HCK4; -. DR PaxDb; 9606-ENSP00000417335; -. DR PeptideAtlas; Q9HCK4; -. DR ProteomicsDB; 81744; -. [Q9HCK4-1] DR ProteomicsDB; 81745; -. [Q9HCK4-2] DR ProteomicsDB; 81746; -. [Q9HCK4-3] DR Antibodypedia; 2693; 284 antibodies from 34 providers. DR DNASU; 6092; -. DR Ensembl; ENST00000461745.5; ENSP00000417164.1; ENSG00000185008.19. [Q9HCK4-1] DR Ensembl; ENST00000487694.7; ENSP00000417335.2; ENSG00000185008.19. [Q9HCK4-3] DR GeneID; 6092; -. DR KEGG; hsa:6092; -. DR UCSC; uc003dpy.5; human. [Q9HCK4-1] DR AGR; HGNC:10250; -. DR CTD; 6092; -. DR DisGeNET; 6092; -. DR GeneCards; ROBO2; -. DR HGNC; HGNC:10250; ROBO2. DR HPA; ENSG00000185008; Tissue enhanced (brain, ovary). DR MalaCards; ROBO2; -. DR MIM; 602431; gene. DR MIM; 610878; phenotype. DR neXtProt; NX_Q9HCK4; -. DR OpenTargets; ENSG00000185008; -. DR Orphanet; 289365; Familial vesicoureteral reflux. DR PharmGKB; PA34621; -. DR VEuPathDB; HostDB:ENSG00000185008; -. DR eggNOG; KOG4222; Eukaryota. DR GeneTree; ENSGT00940000156324; -. DR InParanoid; Q9HCK4; -. DR OMA; IVMKNHD; -. DR OrthoDB; 5396194at2759; -. DR PhylomeDB; Q9HCK4; -. DR TreeFam; TF351053; -. DR PathwayCommons; Q9HCK4; -. DR Reactome; R-HSA-376176; Signaling by ROBO receptors. DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO. DR Reactome; R-HSA-8985801; Regulation of cortical dendrite branching. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9010642; ROBO receptors bind AKAP5. DR SignaLink; Q9HCK4; -. DR SIGNOR; Q9HCK4; -. DR BioGRID-ORCS; 6092; 10 hits in 1135 CRISPR screens. DR ChiTaRS; ROBO2; human. DR EvolutionaryTrace; Q9HCK4; -. DR GeneWiki; ROBO2; -. DR GenomeRNAi; 6092; -. DR Pharos; Q9HCK4; Tbio. DR PRO; PR:Q9HCK4; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9HCK4; Protein. DR Bgee; ENSG00000185008; Expressed in ganglionic eminence and 145 other cell types or tissues. DR ExpressionAtlas; Q9HCK4; baseline and differential. DR GO; GO:0030673; C:axolemma; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008046; F:axon guidance receptor activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA: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:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB. DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB. DR GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; IEP:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB. DR GO; GO:0007417; P:central nervous system development; NAS:UniProtKB. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR GO; GO:0003272; P:endocardial cushion formation; ISS:BHF-UCL. DR GO; GO:0003129; P:heart induction; ISS:BHF-UCL. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB. DR GO; GO:0001656; P:metanephros development; ISS:UniProtKB. DR GO; GO:0050925; P:negative regulation of negative chemotaxis; IDA:UniProtKB. DR GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB. DR GO; GO:0021891; P:olfactory bulb interneuron development; ISS:UniProtKB. 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:0045747; P:positive regulation of Notch signaling pathway; ISS:BHF-UCL. DR GO; GO:0003184; P:pulmonary valve morphogenesis; ISS:BHF-UCL. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB. DR GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB. DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL. DR CDD; cd00063; FN3; 3. DR CDD; cd07693; IgC_1_Robo; 1. DR CDD; cd05726; IgI_4_Robo; 1. DR CDD; cd20952; IgI_5_Robo; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR44170; PROTEIN SIDEKICK; 1. DR PANTHER; PTHR44170:SF52; ROUNDABOUT HOMOLOG 2; 1. DR Pfam; PF00041; fn3; 3. DR Pfam; PF07679; I-set; 2. DR Pfam; PF13927; Ig_3; 3. DR SMART; SM00060; FN3; 3. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 5. DR SMART; SM00406; IGv; 3. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS50835; IG_LIKE; 5. DR Genevisible; Q9HCK4; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chemotaxis; Chromosomal rearrangement; KW Developmental protein; Differentiation; Disease variant; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..1378 FT /note="Roundabout homolog 2" FT /id="PRO_0000031036" FT TOPO_DOM 22..859 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 860..880 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 881..1378 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 31..127 FT /note="Ig-like C2-type 1" FT DOMAIN 133..220 FT /note="Ig-like C2-type 2" FT DOMAIN 225..309 FT /note="Ig-like C2-type 3" FT DOMAIN 314..409 FT /note="Ig-like C2-type 4" FT DOMAIN 418..504 FT /note="Ig-like C2-type 5" FT DOMAIN 524..618 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 637..735 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 739..836 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 603..625 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1032..1084 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1124..1156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1215..1348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 603..617 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1141..1156 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1240..1284 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1292..1313 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1324..1343 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1154 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7TPD3" FT MOD_RES 1156 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TPD3" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 426 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 752 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 782 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 789 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 845 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 52..110 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 154..203 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 246..293 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 335..391 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 439..488 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..20 FT /note="MSLLMFTQLLLCGFLYVRVD -> MARRHERVTRRMWTWAPGLLMMTVVFWG FT HQGNGQGQ (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_043394" FT VAR_SEQ 1186..1378 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010647" FT VARIANT 945 FT /note="I -> T (in VUR2; dbSNP:rs267607014)" FT /evidence="ECO:0000269|PubMed:17357069" FT /id="VAR_032960" FT VARIANT 1236 FT /note="A -> T (in VUR2; dbSNP:rs267607015)" FT /evidence="ECO:0000269|PubMed:17357069" FT /id="VAR_032961" FT CONFLICT 497 FT /note="T -> A (in Ref. 5)" FT /evidence="ECO:0000305" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:6I9S" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 199..207 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 210..213 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 217..229 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 234..240 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 255..260 FT /evidence="ECO:0007829|PDB:6I9S" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 278..282 FT /evidence="ECO:0007829|PDB:6I9S" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 289..297 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 300..311 FT /evidence="ECO:0007829|PDB:6I9S" FT STRAND 312..318 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 336..341 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 345..349 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 376..378 FT /evidence="ECO:0007829|PDB:5NOI" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 387..394 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 399..409 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 419..422 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 448..453 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 456..458 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 464..467 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 473..477 FT /evidence="ECO:0007829|PDB:5NOI" FT HELIX 480..482 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 484..492 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 495..508 FT /evidence="ECO:0007829|PDB:5NOI" FT STRAND 529..533 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 538..541 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 554..561 FT /evidence="ECO:0007829|PDB:1UEM" FT TURN 562..564 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 565..575 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 577..582 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 590..599 FT /evidence="ECO:0007829|PDB:1UEM" FT STRAND 602..606 FT /evidence="ECO:0007829|PDB:1UEM" FT HELIX 630..636 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 639..641 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 651..660 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 667..679 FT /evidence="ECO:0007829|PDB:1UJT" FT TURN 680..682 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 685..688 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 696..701 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 704..718 FT /evidence="ECO:0007829|PDB:1UJT" FT STRAND 727..731 FT /evidence="ECO:0007829|PDB:1UJT" SQ SEQUENCE 1378 AA; 151200 MW; 60F7CE3E53622B50 CRC64; MSLLMFTQLL LCGFLYVRVD GSRLRQEDFP PRIVEHPSDV IVSKGEPTTL NCKAEGRPTP TIEWYKDGER VETDKDDPRS HRMLLPSGSL FFLRIVHGRR SKPDEGSYVC VARNYLGEAV SRNASLEVAL LRDDFRQNPT DVVVAAGEPA ILECQPPRGH PEPTIYWKKD KVRIDDKEER ISIRGGKLMI SNTRKSDAGM YTCVGTNMVG ERDSDPAELT VFERPTFLRR PINQVVLEEE AVEFRCQVQG DPQPTVRWKK DDADLPRGRY DIKDDYTLRI KKTMSTDEGT YMCIAENRVG KMEASATLTV RAPPQFVVRP RDQIVAQGRT VTFPCETKGN PQPAVFWQKE GSQNLLFPNQ PQQPNSRCSV SPTGDLTITN IQRSDAGYYI CQALTVAGSI LAKAQLEVTD VLTDRPPPII LQGPANQTLA VDGTALLKCK ATGDPLPVIS WLKEGFTFPG RDPRATIQEQ GTLQIKNLRI SDTGTYTCVA TSSSGETSWS AVLDVTESGA TISKNYDLSD LPGPPSKPQV TDVTKNSVTL SWQPGTPGTL PASAYIIEAF SQSVSNSWQT VANHVKTTLY TVRGLRPNTI YLFMVRAINP QGLSDPSPMS DPVRTQDISP PAQGVDHRQV QKELGDVLVR LHNPVVLTPT TVQVTWTVDR QPQFIQGYRV MYRQTSGLQA TSSWQNLDAK VPTERSAVLV NLKKGVTYEI KVRPYFNEFQ GMDSESKTVR TTEEAPSAPP QSVTVLTVGS YNSTSISVSW DPPPPDHQNG IIQEYKIWCL GNETRFHINK TVDAAIRSVI IGGLFPGIQY RVEVAASTSA GVGVKSEPQP IIIGRRNEVV ITENNNSITE QITDVVKQPA FIAGIGGACW VILMGFSIWL YWRRKKRKGL SNYAVTFQRG DGGLMSNGSR PGLLNAGDPS YPWLADSWPA TSLPVNNSNS GPNEIGNFGR GDVLPPVPGQ GDKTATMLSD GAIYSSIDFT TKTSYNSSSQ ITQATPYATT QILHSNSIHE LAVDLPDPQW KSSIQQKTDL MGFGYSLPDQ NKGNNGGKGG KKKKNKNSSK PQKNNGSTWA NVPLPPPPVQ PLPGTELEHY AVEQQENGYD SDSWCPPLPV QTYLHQGLED ELEEDDDRVP TPPVRGVASS PAISFGQQST ATLTPSPREE MQPMLQAHLD ELTRAYQFDI AKQTWHIQSN NQPPQPPVPP LGYVSGALIS DLETDVADDD ADDEEEALEI PRPLRALDQT PGSSMDNLDS SVTGKAFTSS QRPRPTSPFS TDSNTSAALS QSQRPRPTKK HKGGRMDQQP ALPHRREGMT DEEALVPYSK PSFPSPGGHS SSGTASSKGS TGPRKTEVLR AGHQRNASDL LDIGYMGSNS QGQFTGEL //