UNC5C_HUMAN
ID UNC5C_HUMAN Reviewed; 931 AA.
AC O95185; Q8IUT0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Netrin receptor UNC5C;
DE AltName: Full=Protein unc-5 homolog 3;
DE AltName: Full=Protein unc-5 homolog C;
DE Flags: Precursor;
GN Name=UNC5C; Synonyms=UNC5H3;
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), TISSUE SPECIFICITY, AND VARIANT
RP THR-721.
RC TISSUE=Brain;
RX PubMed=9782087; DOI=10.1006/geno.1998.5425;
RA Ackerman S.L., Knowles B.B.;
RT "Cloning and mapping of the UNC5C gene to human chromosome 4q21-q23.";
RL Genomics 52:205-208(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [4]
RP DOWN-REGULATION IN CANCER.
RX PubMed=12655055; DOI=10.1073/pnas.0738063100;
RA Thiebault K., Mazelin L., Pays L., Llambi F., Joly M.-O., Scoazec J.-Y.,
RA Saurin J.-C., Romeo G., Mehlen P.;
RT "The netrin-1 receptors UNC5H are putative tumor suppressors controlling
RT cell death commitment.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4173-4178(2003).
RN [5]
RP INTERACTION WITH DSCAM.
RX PubMed=22685302; DOI=10.1074/jbc.m112.340174;
RA Purohit A.A., Li W., Qu C., Dwyer T., Shao Q., Guan K.L., Liu G.;
RT "Down syndrome cell adhesion molecule (DSCAM) associates with
RT uncoordinated-5C (UNC5C) in netrin-1-mediated growth cone collapse.";
RL J. Biol. Chem. 287:27126-27138(2012).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN AD, VARIANT AD
RP MET-835, AND CHARACTERIZATION OF VARIANT AD MET-835.
RX PubMed=25419706; DOI=10.1038/nm.3736;
RG Alzheimer's Disease Genetics Consortium;
RA Wetzel-Smith M.K., Hunkapiller J., Bhangale T.R., Srinivasan K.,
RA Maloney J.A., Atwal J.K., Sa S.M., Yaylaoglu M.B., Foreman O., Ortmann W.,
RA Rathore N., Hansen D.V., Tessier-Lavigne M., Mayeux R., Pericak-Vance M.,
RA Haines J., Farrer L.A., Schellenberg G.D., Goate A., Behrens T.W.,
RA Cruchaga C., Watts R.J., Graham R.R.;
RT "A rare mutation in UNC5C predisposes to late-onset Alzheimer's disease and
RT increases neuronal cell death.";
RL Nat. Med. 20:1452-1457(2014).
RN [7]
RP INTERACTION WITH DAPK1, AND CHARACTERIZATION OF VARIANT AD MET-835.
RX PubMed=27068745; DOI=10.1074/jbc.m115.698092;
RA Hashimoto Y., Toyama Y., Kusakari S., Nawa M., Matsuoka M.;
RT "An Alzheimer Disease-linked Rare Mutation Potentiates Netrin Receptor
RT Uncoordinated-5C-induced Signaling That Merges with Amyloid beta Precursor
RT Protein Signaling.";
RL J. Biol. Chem. 291:12282-12293(2016).
RN [8]
RP FUNCTION, AND INTERACTION WITH TUBB3.
RX PubMed=28483977; DOI=10.1523/jneurosci.2617-16.2017;
RA Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.;
RT "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
RT Netrin-1 Repulsion.";
RL J. Neurosci. 37:5620-5633(2017).
CC -!- FUNCTION: Receptor for netrin required for axon guidance (By
CC similarity). Mediates axon repulsion of neuronal growth cones in the
CC developing nervous system upon ligand binding (By similarity).
CC NTN1/Netrin-1 binding might cause dissociation of UNC5C from
CC polymerized TUBB3 in microtubules and thereby lead to increased
CC microtubule dynamics and axon repulsion (PubMed:28483977). Axon
CC repulsion in growth cones may also be caused by its association with
CC DCC that may trigger signaling for repulsion (By similarity). Might
CC also collaborate with DSCAM in NTN1-mediated axon repulsion
CC independently of DCC (By similarity). Also involved in corticospinal
CC tract axon guidance independently of DCC (By similarity). Involved in
CC dorsal root ganglion axon projection towards the spinal cord
CC (PubMed:28483977). It also acts as a dependence receptor required for
CC apoptosis induction when not associated with netrin ligand (By
CC similarity). {ECO:0000250|UniProtKB:O08747,
CC ECO:0000250|UniProtKB:Q761X5, ECO:0000269|PubMed:28483977}.
CC -!- SUBUNIT: Interacts with DCC (via cytoplasmic domain) (By similarity).
CC Interacts (tyrosine phosphorylated form) with PTPN11 (By similarity).
CC Interacts (via extracellular domain) with FLRT3 (via extracellular
CC domain) (By similarity). Interacts (via Ig-like C2-type domain) with
CC DSCAM (via extracellular domain) (PubMed:22685302). Interacts (via
CC death domain) with DAPK1 (PubMed:27068745). Interacts (via cytoplasmic
CC domain) with TUBB3; this interaction is decreased by NTN1/Netrin-1
CC (PubMed:28483977). {ECO:0000250|UniProtKB:O08747,
CC ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:27068745,
CC ECO:0000269|PubMed:28483977}.
CC -!- INTERACTION:
CC O95185; Q13509: TUBB3; NbExp=2; IntAct=EBI-11343380, EBI-350989;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25419706};
CC Single-pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000269|PubMed:25419706}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q761X5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:O08747}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:O08747}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:O08747}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O08747}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:O08747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95185-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95185-2; Sequence=VSP_011700, VSP_011701;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain (PubMed:9782087).
CC Expressed in temporal lobe cortical neurons and in neurons of the
CC hippocampal pyramidal layer (PubMed:25419706). Also expressed in kidney
CC (PubMed:9782087). Not expressed in developing or adult lung
CC (PubMed:9782087). {ECO:0000269|PubMed:25419706,
CC ECO:0000269|PubMed:9782087}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage
CC does not take place when the receptor is associated with netrin ligand.
CC Its cleavage by caspases is required to induce apoptosis.
CC {ECO:0000250|UniProtKB:Q761X5}.
CC -!- PTM: Phosphorylated on different cytoplasmic tyrosine residues.
CC Phosphorylation of Tyr-568 leads to an interaction with PTPN11
CC phosphatase, suggesting that its activity is regulated by
CC phosphorylation/dephosphorylation. Tyrosine phosphorylation is netrin-
CC dependent. {ECO:0000250|UniProtKB:O08747}.
CC -!- DISEASE: Alzheimer disease (AD) [MIM:104300]: Alzheimer disease is a
CC neurodegenerative disorder characterized by progressive dementia, loss
CC of cognitive abilities, and deposition of fibrillar amyloid proteins as
CC intraneuronal neurofibrillary tangles, extracellular amyloid plaques
CC and vascular amyloid deposits. The major constituents of these plaques
CC are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42,
CC that are produced by the proteolysis of the transmembrane APP protein.
CC The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved
CC products, such as C31, are also implicated in neuronal death.
CC {ECO:0000269|PubMed:25419706, ECO:0000269|PubMed:27068745}.
CC Note=Disease susceptibility may be associated with variants affecting
CC the gene represented in this entry.
CC -!- MISCELLANEOUS: Down-regulated in multiple cancers including colorectal,
CC breast, ovary, uterus, stomach, lung, or kidney cancers.
CC {ECO:0000269|PubMed:12655055}.
CC -!- SIMILARITY: Belongs to the unc-5 family. {ECO:0000305}.
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DR EMBL; AF055634; AAC67491.1; -; mRNA.
DR EMBL; AC098584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041156; AAH41156.1; -; mRNA.
DR CCDS; CCDS3643.1; -. [O95185-1]
DR RefSeq; NP_003719.3; NM_003728.3. [O95185-1]
DR AlphaFoldDB; O95185; -.
DR SMR; O95185; -.
DR BioGRID; 114186; 29.
DR DIP; DIP-46276N; -.
DR IntAct; O95185; 5.
DR STRING; 9606.ENSP00000406022; -.
DR GlyGen; O95185; 2 sites.
DR iPTMnet; O95185; -.
DR PhosphoSitePlus; O95185; -.
DR BioMuta; UNC5C; -.
DR jPOST; O95185; -.
DR MassIVE; O95185; -.
DR PaxDb; O95185; -.
DR PeptideAtlas; O95185; -.
DR PRIDE; O95185; -.
DR ProteomicsDB; 50694; -. [O95185-1]
DR ProteomicsDB; 50695; -. [O95185-2]
DR Antibodypedia; 2665; 273 antibodies from 34 providers.
DR DNASU; 8633; -.
DR Ensembl; ENST00000453304.6; ENSP00000406022.1; ENSG00000182168.15. [O95185-1]
DR Ensembl; ENST00000506749.5; ENSP00000426153.1; ENSG00000182168.15. [O95185-2]
DR GeneID; 8633; -.
DR KEGG; hsa:8633; -.
DR MANE-Select; ENST00000453304.6; ENSP00000406022.1; NM_003728.4; NP_003719.3.
DR UCSC; uc003hto.4; human. [O95185-1]
DR CTD; 8633; -.
DR DisGeNET; 8633; -.
DR GeneCards; UNC5C; -.
DR HGNC; HGNC:12569; UNC5C.
DR HPA; ENSG00000182168; Tissue enhanced (brain).
DR MalaCards; UNC5C; -.
DR MIM; 104300; phenotype.
DR MIM; 603610; gene.
DR neXtProt; NX_O95185; -.
DR NIAGADS; ENSG00000182168; -.
DR OpenTargets; ENSG00000182168; -.
DR PharmGKB; PA37206; -.
DR VEuPathDB; HostDB:ENSG00000182168; -.
DR eggNOG; KOG1480; Eukaryota.
DR GeneTree; ENSGT00950000182815; -.
DR HOGENOM; CLU_014383_2_1_1; -.
DR InParanoid; O95185; -.
DR OMA; CECQAWS; -.
DR OrthoDB; 334938at2759; -.
DR PhylomeDB; O95185; -.
DR TreeFam; TF316767; -.
DR PathwayCommons; O95185; -.
DR Reactome; R-HSA-418886; Netrin mediated repulsion signals.
DR SignaLink; O95185; -.
DR SIGNOR; O95185; -.
DR BioGRID-ORCS; 8633; 6 hits in 1064 CRISPR screens.
DR ChiTaRS; UNC5C; human.
DR GeneWiki; UNC5C; -.
DR GenomeRNAi; 8633; -.
DR Pharos; O95185; Tbio.
DR PRO; PR:O95185; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O95185; protein.
DR Bgee; ENSG00000182168; Expressed in corpus callosum and 132 other tissues.
DR ExpressionAtlas; O95185; baseline and differential.
DR Genevisible; O95185; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005042; F:netrin receptor activity; IBA:GO_Central.
DR GO; GO:0005043; F:netrin receptor activity involved in chemorepulsion; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IPI:UniProtKB.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; TAS:ProtInc.
DR GO; GO:0061643; P:chemorepulsion of axon; ISS:UniProtKB.
DR GO; GO:1990791; P:dorsal root ganglion development; IDA:UniProtKB.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0051094; P:positive regulation of developmental process; IEA:Ensembl.
DR GO; GO:2000243; P:positive regulation of reproductive process; IEA:Ensembl.
DR GO; GO:2001222; P:regulation of neuron migration; IEA:Ensembl.
DR CDD; cd08799; Death_UNC5C; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.20.100.10; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR042154; Death_UNC5C.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR037936; UNC5.
DR InterPro; IPR033772; UPA.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR12582; PTHR12582; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00090; TSP_1; 2.
DR Pfam; PF17217; UPA; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00209; TSP1; 2.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF82895; SSF82895; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Alzheimer disease; Amyloidosis; Apoptosis;
KW Cell membrane; Cell projection; Developmental protein; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Neurodegeneration;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..931
FT /note="Netrin receptor UNC5C"
FT /id="PRO_0000036075"
FT TOPO_DOM 41..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 62..159
FT /note="Ig-like"
FT DOMAIN 161..256
FT /note="Ig-like C2-type"
FT DOMAIN 260..314
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 316..368
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 530..673
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 850..929
FT /note="Death"
FT REGION 402..931
FT /note="Required for netrin-mediated axon repulsion of
FT neuronal growth cones"
FT /evidence="ECO:0000250|UniProtKB:O08747"
FT REGION 694..712
FT /note="Interaction with DCC"
FT /evidence="ECO:0000250|UniProtKB:O08747"
FT SITE 415..416
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q761X5"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08747"
FT MOD_RES 568
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08747"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..144
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 95..142
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 188..239
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 272..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 276..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 287..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 328..362
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 332..367
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 340..352
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT VAR_SEQ 370
FT /note="T -> SFIYPISTEQRTQNEYGFSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011700"
FT VAR_SEQ 579..931
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011701"
FT VARIANT 37
FT /note="G -> V (in dbSNP:rs2306715)"
FT /id="VAR_019731"
FT VARIANT 721
FT /note="M -> T (in dbSNP:rs2289043)"
FT /evidence="ECO:0000269|PubMed:9782087"
FT /id="VAR_019732"
FT VARIANT 835
FT /note="T -> M (in AD; associated with susceptibility to
FT late-onset disease; increased susceptibility to neuronal
FT cell death; dbSNP:rs137875858)"
FT /evidence="ECO:0000269|PubMed:25419706,
FT ECO:0000269|PubMed:27068745"
FT /id="VAR_081368"
FT VARIANT 841
FT /note="A -> T (in dbSNP:rs34585936)"
FT /id="VAR_055327"
FT CONFLICT 219
FT /note="T -> I (in Ref. 3; AAH41156)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="T -> S (in Ref. 1; AAC67491)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="Q -> K (in Ref. 1; AAC67491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 103146 MW; 98A95995129532A7 CRC64;
MRKGLRATAA RCGLGLGYLL QMLVLPALAL LSASGTGSAA QDDDFFHELP ETFPSDPPEP
LPHFLIEPEE AYIVKNKPVN LYCKASPATQ IYFKCNSEWV HQKDHIVDER VDETSGLIVR
EVSIEISRQQ VEELFGPEDY WCQCVAWSSA GTTKSRKAYV RIAYLRKTFE QEPLGKEVSL
EQEVLLQCRP PEGIPVAEVE WLKNEDIIDP VEDRNFYITI DHNLIIKQAR LSDTANYTCV
AKNIVAKRKS TTATVIVYVN GGWSTWTEWS VCNSRCGRGY QKRTRTCTNP APLNGGAFCE
GQSVQKIACT TLCPVDGRWT PWSKWSTCGT ECTHWRRREC TAPAPKNGGK DCDGLVLQSK
NCTDGLCMQT APDSDDVALY VGIVIAVIVC LAISVVVALF VYRKNHRDFE SDIIDSSALN
GGFQPVNIKA ARQDLLAVPP DLTSAAAMYR GPVYALHDVS DKIPMTNSPI LDPLPNLKIK
VYNTSGAVTP QDDLSEFTSK LSPQMTQSLL ENEALSLKNQ SLARQTDPSC TAFGSFNSLG
GHLIVPNSGV SLLIPAGAIP QGRVYEMYVT VHRKETMRPP MDDSQTLLTP VVSCGPPGAL
LTRPVVLTMH HCADPNTEDW KILLKNQAAQ GQWEDVVVVG EENFTTPCYI QLDAEACHIL
TENLSTYALV GHSTTKAAAK RLKLAIFGPL CCSSLEYSIR VYCLDDTQDA LKEILHLERQ
MGGQLLEEPK ALHFKGSTHN LRLSIHDIAH SLWKSKLLAK YQEIPFYHVW SGSQRNLHCT
FTLERFSLNT VELVCKLCVR QVEGEGQIFQ LNCTVSEEPT GIDLPLLDPA NTITTVTGPS
AFSIPLPIRQ KLCSSLDAPQ TRGHDWRMLA HKLNLDRYLN YFATKSSPTG VILDLWEAQN
FPDGNLSMLA AVLEEMGRHE TVVSLAAEGQ Y
