ROBO2_HUMAN
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 03-AUG-2022, entry version 192.
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};
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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; 35.
DR IntAct; Q9HCK4; 30.
DR MINT; Q9HCK4; -.
DR STRING; 9606.ENSP00000417335; -.
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; Q9HCK4; -.
DR PeptideAtlas; Q9HCK4; -.
DR PRIDE; Q9HCK4; -.
DR ProteomicsDB; 81744; -. [Q9HCK4-1]
DR ProteomicsDB; 81745; -. [Q9HCK4-2]
DR ProteomicsDB; 81746; -. [Q9HCK4-3]
DR Antibodypedia; 2693; 262 antibodies from 34 providers.
DR DNASU; 6092; -.
DR Ensembl; ENST00000461745.5; ENSP00000417164.1; ENSG00000185008.17. [Q9HCK4-1]
DR Ensembl; ENST00000487694.7; ENSP00000417335.2; ENSG00000185008.17. [Q9HCK4-3]
DR GeneID; 6092; -.
DR KEGG; hsa:6092; -.
DR UCSC; uc003dpy.5; human. [Q9HCK4-1]
DR CTD; 6092; -.
DR DisGeNET; 6092; -.
DR GeneCards; ROBO2; -.
DR HGNC; HGNC:10250; ROBO2.
DR HPA; ENSG00000185008; Tissue enhanced (brain, retina).
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; GVIVMKN; -.
DR OrthoDB; 45439at2759; -.
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; 9 hits in 1058 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 144 other tissues.
DR ExpressionAtlas; Q9HCK4; baseline and differential.
DR Genevisible; Q9HCK4; HS.
DR GO; GO:0030673; C:axolemma; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008046; F:axon guidance receptor activity; ISS:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
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: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: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:0035481; P:positive regulation of Notch signaling pathway involved in heart induction; 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 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 Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 4.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
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; 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
