ROBO4_HUMAN
ID ROBO4_HUMAN Reviewed; 1007 AA.
AC Q8WZ75; A8K154; Q14DU7; Q8TEG1; Q96JV6; Q9H718; Q9NWJ8;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Roundabout homolog 4;
DE AltName: Full=Magic roundabout;
DE Flags: Precursor;
GN Name=ROBO4; ORFNames=UNQ421/PRO3674;
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 TISSUE SPECIFICITY.
RX PubMed=11944987; DOI=10.1006/geno.2002.6745;
RA Huminiecki L., Gorn M., Suchting S., Poulsom R., Bicknell R.;
RT "Magic roundabout is a new member of the roundabout receptor family that is
RT endothelial specific and expressed at sites of active angiogenesis.";
RL Genomics 79:547-552(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-1007 (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Adipose tissue, Brain, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and 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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP GLYCOSYLATION AT ASN-246.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, VARIANTS AOVD3 CYS-64; THR-95; MET-232;
RP ALA-247; SER-280; GLN-411; VAL-510; 568-ARG--SER-1007 DEL; HIS-622 AND
RP LEU-749, AND CHARACTERIZATION OF VARIANT AOVD3 CYS-64.
RX PubMed=30455415; DOI=10.1038/s41588-018-0265-y;
RG Baylor-Hopkins Center for Mendelian Genomics;
RG MIBAVA Leducq Consortium;
RA Gould R.A., Aziz H., Woods C.E., Seman-Senderos M.A., Sparks E., Preuss C.,
RA Wuennemann F., Bedja D., Moats C.R., McClymont S.A., Rose R., Sobreira N.,
RA Ling H., MacCarrick G., Kumar A.A., Luyckx I., Cannaerts E.,
RA Verstraeten A., Bjoerk H.M., Lehsau A.C., Jaskula-Ranga V., Lauridsen H.,
RA Shah A.A., Bennett C.L., Ellinor P.T., Lin H., Isselbacher E.M.,
RA Lino Cardenas C.L., Butcher J.T., Hughes G.C., Lindsay M.E., Mertens L.,
RA Franco-Cereceda A., Verhagen J.M.A., Wessels M., Mohamed S.A., Eriksson P.,
RA Mital S., Van Laer L., Loeys B.L., Andelfinger G., McCallion A.S.,
RA Dietz H.C.;
RT "ROBO4 variants predispose individuals to bicuspid aortic valve and
RT thoracic aortic aneurysm.";
RL Nat. Genet. 51:42-50(2019).
CC -!- FUNCTION: Receptor for Slit proteins, at least for SLIT2, and seems to
CC be involved in angiogenesis and vascular patterning. May mediate the
CC inhibition of primary endothelial cell migration by Slit proteins (By
CC similarity). Involved in the maintenance of endothelial barrier
CC organization and function (PubMed:30455415). {ECO:0000250,
CC ECO:0000269|PubMed:30455415}.
CC -!- SUBUNIT: Interacts with SLIT2 and ENAH. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WZ75; Q96LK0: CEP19; NbExp=3; IntAct=EBI-6508018, EBI-741885;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WZ75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WZ75-2; Sequence=VSP_010658, VSP_010659;
CC Name=3;
CC IsoId=Q8WZ75-3; Sequence=VSP_010654, VSP_010657;
CC -!- TISSUE SPECIFICITY: Specifically expressed in endothelial cells.
CC Expressed in endothelial and intimal cells of the ascending aorta
CC (PubMed:30455415). {ECO:0000269|PubMed:11944987,
CC ECO:0000269|PubMed:30455415}.
CC -!- DISEASE: Aortic valve disease 3 (AOVD3) [MIM:618496]: A common defect
CC in the aortic valve in which two rather than three leaflets are
CC present. It is often associated with aortic valve calcification,
CC stenosis and insufficiency. In extreme cases, the blood flow may be so
CC restricted that the left ventricle fails to grow, resulting in
CC hypoplastic left heart syndrome. AOVD3 features are bicuspid aortic
CC valve, aortic valve stenosis, and ascending aortic aneurysm. Some
CC patients have atrial septal defects. AOVD3 inheritance is autosomal
CC dominant with incomplete penetrance. {ECO:0000269|PubMed:30455415}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64643.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55411.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF361473; AAL31867.1; -; mRNA.
DR EMBL; AY358083; AAQ88450.1; -; mRNA.
DR EMBL; AK000805; BAA91382.1; ALT_INIT; mRNA.
DR EMBL; AK025195; BAB15082.1; ALT_INIT; mRNA.
DR EMBL; AK027852; BAB55411.1; ALT_FRAME; mRNA.
DR EMBL; AK074163; BAB84989.1; -; mRNA.
DR EMBL; AK289769; BAF82458.1; -; mRNA.
DR EMBL; BC039602; AAH39602.1; -; mRNA.
DR EMBL; BC064643; AAH64643.1; ALT_INIT; mRNA.
DR EMBL; BC111562; AAI11563.1; -; mRNA.
DR EMBL; BC111748; AAI11749.1; -; mRNA.
DR CCDS; CCDS8455.1; -. [Q8WZ75-1]
DR RefSeq; NP_001288017.1; NM_001301088.1.
DR RefSeq; NP_061928.4; NM_019055.5. [Q8WZ75-1]
DR AlphaFoldDB; Q8WZ75; -.
DR SMR; Q8WZ75; -.
DR BioGRID; 120025; 8.
DR CORUM; Q8WZ75; -.
DR IntAct; Q8WZ75; 6.
DR STRING; 9606.ENSP00000304945; -.
DR GlyConnect; 2004; 4 N-Linked glycans (1 site).
DR GlyGen; Q8WZ75; 6 sites, 4 N-linked glycans (1 site), 2 O-linked glycans (1 site).
DR iPTMnet; Q8WZ75; -.
DR PhosphoSitePlus; Q8WZ75; -.
DR BioMuta; ROBO4; -.
DR DMDM; 49036490; -.
DR jPOST; Q8WZ75; -.
DR MassIVE; Q8WZ75; -.
DR PaxDb; Q8WZ75; -.
DR PeptideAtlas; Q8WZ75; -.
DR PRIDE; Q8WZ75; -.
DR ProteomicsDB; 75232; -. [Q8WZ75-1]
DR ProteomicsDB; 75233; -. [Q8WZ75-2]
DR ProteomicsDB; 75234; -. [Q8WZ75-3]
DR Antibodypedia; 32921; 444 antibodies from 30 providers.
DR DNASU; 54538; -.
DR Ensembl; ENST00000306534.8; ENSP00000304945.3; ENSG00000154133.15. [Q8WZ75-1]
DR GeneID; 54538; -.
DR KEGG; hsa:54538; -.
DR MANE-Select; ENST00000306534.8; ENSP00000304945.3; NM_019055.6; NP_061928.4.
DR UCSC; uc001qbg.4; human. [Q8WZ75-1]
DR CTD; 54538; -.
DR DisGeNET; 54538; -.
DR GeneCards; ROBO4; -.
DR HGNC; HGNC:17985; ROBO4.
DR HPA; ENSG00000154133; Low tissue specificity.
DR MalaCards; ROBO4; -.
DR MIM; 607528; gene.
DR MIM; 618496; phenotype.
DR neXtProt; NX_Q8WZ75; -.
DR OpenTargets; ENSG00000154133; -.
DR PharmGKB; PA34622; -.
DR VEuPathDB; HostDB:ENSG00000154133; -.
DR eggNOG; KOG4222; Eukaryota.
DR GeneTree; ENSGT00940000161382; -.
DR InParanoid; Q8WZ75; -.
DR OMA; WEPPPHE; -.
DR OrthoDB; 242944at2759; -.
DR PhylomeDB; Q8WZ75; -.
DR TreeFam; TF351053; -.
DR PathwayCommons; Q8WZ75; -.
DR SignaLink; Q8WZ75; -.
DR SIGNOR; Q8WZ75; -.
DR BioGRID-ORCS; 54538; 14 hits in 1063 CRISPR screens.
DR GeneWiki; ROBO4; -.
DR GenomeRNAi; 54538; -.
DR Pharos; Q8WZ75; Tbio.
DR PRO; PR:Q8WZ75; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8WZ75; protein.
DR Bgee; ENSG00000154133; Expressed in lower lobe of lung and 179 other tissues.
DR ExpressionAtlas; Q8WZ75; baseline and differential.
DR Genevisible; Q8WZ75; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IGI:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; NAS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 4.
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 Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Developmental protein; Differentiation;
KW Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1007
FT /note="Roundabout homolog 4"
FT /id="PRO_0000031040"
FT DOMAIN 32..131
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 248..345
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 347..442
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 531..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C310"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 24..133
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010654"
FT VAR_SEQ 813..1007
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010657"
FT VAR_SEQ 932..933
FT /note="DA -> GM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010658"
FT VAR_SEQ 934..1007
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010659"
FT VARIANT 54
FT /note="Q -> R (in dbSNP:rs59648931)"
FT /id="VAR_062146"
FT VARIANT 64
FT /note="R -> C (in AOVD3; loss of endothelial barrier
FT function in a dextran permeability assay;
FT dbSNP:rs201393279)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083093"
FT VARIANT 95
FT /note="A -> T (in AOVD3; unknown pathological significance;
FT dbSNP:rs138370967)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083094"
FT VARIANT 232
FT /note="T -> M (in AOVD3; unknown pathological significance;
FT dbSNP:rs150700978)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083095"
FT VARIANT 247
FT /note="V -> A (in AOVD3; unknown pathological significance;
FT dbSNP:rs779392207)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083096"
FT VARIANT 280
FT /note="Y -> S (in AOVD3; unknown pathological significance;
FT dbSNP:rs755747435)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083097"
FT VARIANT 411
FT /note="H -> Q (in AOVD3; unknown pathological significance;
FT dbSNP:rs1565326476)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083098"
FT VARIANT 510
FT /note="D -> V (in AOVD3; unknown pathological significance;
FT dbSNP:rs1565325937)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083099"
FT VARIANT 568..1007
FT /note="Missing (in AOVD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083100"
FT VARIANT 622
FT /note="D -> H (in AOVD3; unknown pathological significance;
FT dbSNP:rs138111911)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083101"
FT VARIANT 669
FT /note="R -> Q (in dbSNP:rs4408324)"
FT /id="VAR_053644"
FT VARIANT 749
FT /note="A -> L (in AOVD3; unknown pathological significance;
FT requires 2 nucleotide substitutions; dbSNP:rs1565322176)"
FT /evidence="ECO:0000269|PubMed:30455415"
FT /id="VAR_083102"
FT CONFLICT 175
FT /note="G -> E (in Ref. 3; BAB55411)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="H -> L (in Ref. 3; BAA91382)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="Q -> P (in Ref. 3; BAB55411)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="G -> D (in Ref. 3; BAB84989)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="P -> L (in Ref. 3; BAB15082)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="L -> F (in Ref. 3; BAB15082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 107457 MW; E43F246C59BE1415 CRC64;
MGSGGDSLLG GRGSLPLLLL LIMGGMAQDS PPQILVHPQD QLFQGPGPAR MSCQASGQPP
PTIRWLLNGQ PLSMVPPDPH HLLPDGTLLL LQPPARGHAH DGQALSTDLG VYTCEASNRL
GTAVSRGARL SVAVLREDFQ IQPRDMVAVV GEQFTLECGP PWGHPEPTVS WWKDGKPLAL
QPGRHTVSGG SLLMARAEKS DEGTYMCVAT NSAGHRESRA ARVSIQEPQD YTEPVELLAV
RIQLENVTLL NPDPAEGPKP RPAVWLSWKV SGPAAPAQSY TALFRTQTAP GGQGAPWAEE
LLAGWQSAEL GGLHWGQDYE FKVRPSSGRA RGPDSNVLLL RLPEKVPSAP PQEVTLKPGN
GTVFVSWVPP PAENHNGIIR GYQVWSLGNT SLPPANWTVV GEQTQLEIAT HMPGSYCVQV
AAVTGAGAGE PSRPVCLLLE QAMERATQEP SEHGPWTLEQ LRATLKRPEV IATCGVALWL
LLLGTAVCIH RRRRARVHLG PGLYRYTSED AILKHRMDHS DSQWLADTWR STSGSRDLSS
SSSLSSRLGA DARDPLDCRR SLLSWDSRSP GVPLLPDTST FYGSLIAELP SSTPARPSPQ
VPAVRRLPPQ LAQLSSPCSS SDSLCSRRGL SSPRLSLAPA EAWKAKKKQE LQHANSSPLL
RGSHSLELRA CELGNRGSKN LSQSPGAVPQ ALVAWRALGP KLLSSSNELV TRHLPPAPLF
PHETPPTQSQ QTQPPVAPQA PSSILLPAAP IPILSPCSPP SPQASSLSGP SPASSRLSSS
SLSSLGEDQD SVLTPEEVAL CLELSEGEET PRNSVSPMPR APSPPTTYGY ISVPTASEFT
DMGRTGGGVG PKGGVLLCPP RPCLTPTPSE GSLANGWGSA SEDNAASARA SLVSSSDGSF
LADAHFARAL AVAVDSFGFG LEPREADCVF IDASSPPSPR DEIFLTPNLS LPLWEWRPDW
LEDMEVSHTQ RLGRGMPPWP PDSQISSQRS QLHCRMPKAG ASPVDYS
