ID   ROBO1_MOUSE             Reviewed;        1612 AA.
AC   O89026;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Roundabout homolog 1;
DE   Flags: Precursor;
GN   Name=Robo1; Synonyms=Dutt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Wu M.C., Lowe N., Fordham R., Rabbitts P.;
RT   "The mouse homologue of human DUTT1/H-robo1 gene: protein sequence and
RT   chromosomal location.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   POSSIBLE FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11734623; DOI=10.1073/pnas.251407098;
RA   Xian J., Clark K.J., Fordham R., Pannell R., Rabbitts T.H., Rabbitts P.H.;
RT   "Inadequate lung development and bronchial hyperplasia in mice with a
RT   targeted deletion in the Dutt1/Robo1 gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:15062-15066(2001).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15091338; DOI=10.1016/s0896-6273(04)00179-5;
RA   Long H., Sabatier C., Ma L., Plump A., Yuan W., Ornitz D.M., Tamada A.,
RA   Murakami F., Goodman C.S., Tessier-Lavigne M.;
RT   "Conserved roles for slit and robo proteins in midline commissural axon
RT   guidance.";
RL   Neuron 42:213-223(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
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   [5]
RP   INTERACTION WITH SLIT1.
RX   PubMed=10433822; DOI=10.1006/dbio.1999.9371;
RA   Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.;
RT   "The mouse SLIT family: secreted ligands for ROBO expressed in patterns
RT   that suggest a role in morphogenesis and axon guidance.";
RL   Dev. Biol. 212:290-306(1999).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12123796; DOI=10.1016/s0014-5793(02)02904-6;
RA   Clark K., Hammond E., Rabbitts P.;
RT   "Temporal and spatial expression of two isoforms of the Dutt1/Robo1 gene in
RT   mouse development.";
RL   FEBS Lett. 523:12-16(2002).
RN   [7]
RP   UBIQUITINATION, AND INTERACTION WITH USP33.
RX   PubMed=19684588; DOI=10.1038/nn.2382;
RA   Yuasa-Kawada J., Kinoshita-Kawada M., Wu G., Rao Y., Wu J.Y.;
RT   "Midline crossing and Slit responsiveness of commissural axons require
RT   USP33.";
RL   Nat. Neurosci. 12:1087-1089(2009).
RN   [8]
RP   INTERACTION WITH USP33.
RX   PubMed=19706539; DOI=10.1073/pnas.0801262106;
RA   Yuasa-Kawada J., Kinoshita-Kawada M., Rao Y., Wu J.Y.;
RT   "Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in
RT   inhibiting breast cancer cell migration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:14530-14535(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   INTERACTION WITH FLRT3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
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   [11]
RP   MUTAGENESIS OF ILE-270.
RX   PubMed=35227688; DOI=10.1016/j.kint.2022.01.028;
RG   Genomics England Research Consortium;
RA   Muench J., Engesser M., Schoenauer R., Hamm J.A., Hartig C., Hantmann E.,
RA   Akay G., Pehlivan D., Mitani T., Coban Akdemir Z., Tueysuez B.,
RA   Shirakawa T., Dateki S., Claus L.R., van Eerde A.M., Smol T., Devisme L.,
RA   Franquet H., Attie-Bitach T., Wagner T., Bergmann C., Hoehn A.K., Shril S.,
RA   Pollack A., Wenger T., Scott A.A., Paolucci S., Buchan J., Gabriel G.C.,
RA   Posey J.E., Lupski J.R., Petit F., McCarthy A.A., Pazour G.J., Lo C.W.,
RA   Popp B., Halbritter J.;
RT   "Biallelic pathogenic variants in roundabout guidance receptor 1 associate
RT   with syndromic congenital anomalies of the kidney and urinary tract.";
RL   Kidney Int. 101:1039-1053(2022).
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:10433822, 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 (By similarity). May be required for
CC       lung development (PubMed:11734623). {ECO:0000250|UniProtKB:Q9Y6N7,
CC       ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:11734623,
CC       ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}.
CC   -!- SUBUNIT: Homodimer. Dimerization is mediated by the extracellular
CC       domain and is independent of SLIT liganding (By similarity). Interacts
CC       with SLIT1 (PubMed:10433822) Interacts with SLIT2 (By similarity).
CC       Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-
CC       GAP domain) (By similarity). {ECO:0000250|UniProtKB:Q9Y6N7,
CC       ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:19684588,
CC       ECO:0000269|PubMed:19706539, ECO:0000269|PubMed:24560577}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24560577};
CC       Single-pass type I membrane protein {ECO:0000305}. Cell projection,
CC       axon {ECO:0000269|PubMed:24560577}. 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 (PubMed:24560577).
CC       PRRG4 prevents cell surface location and both colocalize in the
CC       Endoplasmic reticulum/Golgi adjacent to the cell nucleus (By
CC       similarity). {ECO:0000250|UniProtKB:O55005,
CC       ECO:0000269|PubMed:24560577}.
CC   -!- TISSUE SPECIFICITY: Detected in embryonic thalamus neurons (at protein
CC       level) (PubMed:24560577). Expressed in embryonal spinal chord.
CC       Expressed in embryonal lung, and in adult lung bronchial epithelial
CC       cells of large proximal airways. {ECO:0000269|PubMed:12123796,
CC       ECO:0000269|PubMed:15091338, ECO:0000269|PubMed:24560577}.
CC   -!- DEVELOPMENTAL STAGE: Earliest and highest expression at 11 dpc.
CC       Expression is detected in developing somits, brain, neural tube, and
CC       pericardiac mesenchyme. By in situ hybridization is detected in
CC       marginal zones bordering the mitotically active periventricular region,
CC       weakly extending to the ventral aspect impinging on motor neuron
CC       columns. Also detected in the ventral third of the developing neural
CC       tube, and in spinal cord throughout the full length of the neural tube.
CC       Also detected at 17.5 dpc in lung mesenchyme. Expressed at 11.5 dpc in
CC       spinal cord, predominantly localized to postcrossing commissural axons.
CC       {ECO:0000269|PubMed:12123796, ECO:0000269|PubMed:15091338,
CC       ECO:0000269|PubMed:9608531}.
CC   -!- PTM: Ubiquitinated. May be deubiquitinated by USP33.
CC       {ECO:0000269|PubMed:19684588}.
CC   -!- DISRUPTION PHENOTYPE: Mice show defects in commissural axon guidance in
CC       spinal cord including midline recrossing and an altered lateral and
CC       ventral funiculi projection. The phenotype resembles that of a
CC       SLIT1;SLIT2;SLIT3 triple mutant. They also mimick a naturally occurring
CC       human homozygous deletion mutant detected in a small lung cancer cell
CC       line, frequently die at birth by respiratory failure with accompanying
CC       abnormal lung histology. Surviving mice develop bronchial hyperplasia.
CC       {ECO:0000269|PubMed:11734623}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC       {ECO:0000305}.
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DR   EMBL; Y17793; CAA76850.1; -; mRNA.
DR   CCDS; CCDS37376.1; -.
DR   PIR; T30805; T30805.
DR   RefSeq; NP_062286.2; NM_019413.2.
DR   AlphaFoldDB; O89026; -.
DR   SMR; O89026; -.
DR   BioGRID; 202949; 7.
DR   STRING; 10090.ENSMUSP00000023600; -.
DR   GlyConnect; 2687; 1 N-Linked glycan (1 site).
DR   GlyCosmos; O89026; 5 sites, 1 glycan.
DR   GlyGen; O89026; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; O89026; -.
DR   PhosphoSitePlus; O89026; -.
DR   MaxQB; O89026; -.
DR   PaxDb; 10090-ENSMUSP00000023600; -.
DR   ProteomicsDB; 260915; -.
DR   DNASU; 19876; -.
DR   GeneID; 19876; -.
DR   KEGG; mmu:19876; -.
DR   AGR; MGI:1274781; -.
DR   CTD; 6091; -.
DR   MGI; MGI:1274781; Robo1.
DR   eggNOG; KOG4222; Eukaryota.
DR   InParanoid; O89026; -.
DR   OrthoDB; 5396194at2759; -.
DR   PhylomeDB; O89026; -.
DR   Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR   Reactome; R-MMU-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-MMU-8985586; SLIT2:ROBO1 increases RHOA activity.
DR   Reactome; R-MMU-9010553; Regulation of expression of SLITs and ROBOs.
DR   BioGRID-ORCS; 19876; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Robo1; mouse.
DR   PRO; PR:O89026; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O89026; Protein.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008046; F:axon guidance receptor activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030275; F:LRR domain binding; ISO:MGI.
DR   GO; GO:0035904; P:aorta development; IGI:BHF-UCL.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IGI:BHF-UCL.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0016199; P:axon midline choice point recognition; IGI:UniProtKB.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; ISO:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR   GO; GO:0003272; P:endocardial cushion formation; IGI:BHF-UCL.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0003129; P:heart induction; IDA:BHF-UCL.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0050925; P:negative regulation of negative chemotaxis; ISO:MGI.
DR   GO; GO:0051964; P:negative regulation of synapse assembly; ISO:MGI.
DR   GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR   GO; GO:0021891; P:olfactory bulb interneuron development; IGI:UniProtKB.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; IGI:BHF-UCL.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR   GO; GO:0035385; P:Roundabout signaling pathway; ISS:UniProtKB.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IGI:BHF-UCL.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd07693; IgC_1_Robo; 1.
DR   CDD; cd05724; IgI_2_Robo; 1.
DR   CDD; cd05725; IgI_3_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   InterPro; IPR032986; Robo1_Ig-like3.
DR   PANTHER; PTHR45080; CONTACTIN 5; 1.
DR   PANTHER; PTHR45080:SF32; MYOTILIN; 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.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Chemotaxis; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1612
FT                   /note="Roundabout homolog 1"
FT                   /id="PRO_0000031034"
FT   TOPO_DOM        20..858
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        859..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        880..1612
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..125
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          131..218
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          223..307
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          312..407
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          416..502
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..734
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          739..835
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          1045..1068
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1313..1358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1381..1612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1212..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1399..1414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1477..1500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1515..1538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1551..1582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         901
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         909
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         999
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         1016
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         1034
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         1075
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         1201
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   MOD_RES         1258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6N7"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        751
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        781
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        788
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        152..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        244..291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        333..389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        437..486
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   MUTAGEN         270
FT                   /note="I->T: Loss of expression in the kidney of homozygous
FT                   mice. Mutant mice have severe urogenital defects,
FT                   congenital heart defects and craniofacial abnormalities."
FT                   /evidence="ECO:0000269|PubMed:35227688"
SQ   SEQUENCE   1612 AA;  176407 MW;  5F2988C544796B4B CRC64;
     MIAEPAHFYL FGLICLCSGS RLRQEDFPPR IVEHPSDLIV SKGEPATLNC KAEGRPTPTI
     EWYKGGERVE TDKDDPRSHR MLLPSGSLFF LRIVHGRKSR PDEGVYICVA RNYLGEAVSH
     NASLEVAILR DDFRQNPSDV MVAVGEPAVM ECQPPRGHPE PTISWKKDGS PLDDKDERIT
     IRGGKLMITY TRKSDAGKYV CVGTNMVGER ESEVAELTVL ERPSFVKRPS NLAVTVDDSA
     EFKCEARGDP VPTVRWRKDD GELPKSRYEI RDDHTLKIRK VTAGDMGSYT CVAENMVGKA
     EASATLTVQE PPHFVVKPRD QVVALGRTVT FQCEATGNPQ PAIFWRREGS QNLLFSYQPP
     QSSSRFSVSQ TGDLTITNVQ RSDVGYYICQ TLNVAGSIIT KAYLEVTDVI ADRPPPVIRQ
     GPVNQTVAVD GTLILSCVAT GSPAPTILWR KDGVLVSTQD SRIKQLESGV LQIRYAKLGD
     TGRYTCTAST PSGEATWSAY IEVQEFGVPV QPPRPTDPNL IPSAPSKPEV TDVSKNTVTL
     SWQPNLNSGA TPTSYIIEAF SHASGSSWQT AAENVKTETF AIKGLKPNAI YLFLVRAANA
     YGISDPSQIS DPVKTQDVPP TSQGVDHKQV QRELGNVVLH LHNPTILSSS SVEVHWTVDQ
     QSQYIQGYKI LYRPSGASHG ESEWLVFEVR TPTKNSVVIP DLRKGVNYEI KARPFFNEFQ
     GADSEIKFAK TLEEAPSAPP RSVTVSKNDG NGTAILVTWQ PPPEDTQNGM VQEYKVWCLG
     NETKYHINKT VDGSTFSVVI PSLVPGIRYS VEVAASTGAG PGVKSEPQFI QLDSHGNPVS
     PEDQVSLAQQ ISDVVRQPAF IAGIGAACWI ILMVFSIWLY RHRKKRNGLT STYAGIRKVP
     SFTFTPTVTY QRGGEAVSSG GRPGLLNISE PATQPWLADT WPNTGNNHND CSINCCTAGN
     GNSDSNLTTY SRPADCIANY NNQLDNKQTN LMLPESTVYG DVDLSNKINE MKTFNSPNLK
     DGRFVNPSGQ PTPYATTQLI QANLSNNMNN GAGDSSEKHW KPPGQQKPEV APIQYNIMEQ
     NKLNKDYRAN DTIPPTIPYN QSYDQNTGGS YNSSDRGSST SGSQGHKKGA RTPKAPKQGG
     MNWADLLPPP PAHPPPHSNS EEYNMSVDES YDQEMPCPVP PAPMYLQQDE LQEEEDERGP
     TPPVRGAASS PAAVSYSHQS TATLTPSPQE ELQPMLQDCP EDLGHMPHPP DRRRQPVSPP
     PPPRPISPPH TYGYISGPLV SDMDTDAPEE EEDEADMEVA KMQTRRLLLR GLEQTPASSV
     GDLESSVTGS MINGWGSASE EDNISSGRSS VSSSDGSFFT DADFAQAVAA AAEYAGLKVA
     RRQMQDAAGR RHFHASQCPR PTSPVSTDSN MSAVVIQKAR PAKKQKHQPG HLRREAYADD
     LPPPPVPPPA IKSPTVQSKA QLEVRPVMVP KLASIEARTD RSSDRKGGSY KGREALDGRQ
     VTDLRTNPSD PREAQEQPND GKGRGTRQPK RDLPPAKTHL GQEDILPYCR PTFPTSNNPR
     DPSSSSSMSS RGSGSRQREQ ANVGRRNMAE MQVLGGFERG DENNEELEET ES
//