CNTP1_HUMAN
ID CNTP1_HUMAN Reviewed; 1384 AA.
AC P78357;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Contactin-associated protein 1;
DE Short=Caspr;
DE Short=Caspr1;
DE AltName: Full=Neurexin IV;
DE AltName: Full=Neurexin-4;
DE AltName: Full=p190;
DE Flags: Precursor;
GN Name=CNTNAP1; Synonyms=CASPR, NRXN4;
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], AND INTERACTION WITH CONTACTIN.
RC TISSUE=Neuroblastoma;
RX PubMed=9118959; DOI=10.1093/emboj/16.5.978;
RA Peles E., Nativ M., Lustig M., Grumet M., Schilling J., Martinez R.,
RA Plowman G.D., Schlessinger J.;
RT "Identification of a novel contactin-associated transmembrane receptor with
RT multiple domains implicated in protein-protein interactions.";
RL EMBO J. 16:978-988(1997).
RN [2]
RP INVOLVEMENT IN LCCS7, AND FUNCTION.
RX PubMed=24319099; DOI=10.1093/hmg/ddt618;
RA Laquerriere A., Maluenda J., Camus A., Fontenas L., Dieterich K.,
RA Nolent F., Zhou J., Monnier N., Latour P., Gentil D., Heron D.,
RA Desguerres I., Landrieu P., Beneteau C., Delaporte B., Bellesme C.,
RA Baumann C., Capri Y., Goldenberg A., Lyonnet S., Bonneau D., Estournet B.,
RA Quijano-Roy S., Francannet C., Odent S., Saint-Frison M.H., Sigaudy S.,
RA Figarella-Branger D., Gelot A., Mussini J.M., Lacroix C.,
RA Drouin-Garraud V., Malinge M.C., Attie-Bitach T., Bessieres B.,
RA Bonniere M., Encha-Razavi F., Beaufrere A.M., Khung-Savatovsky S.,
RA Perez M.J., Vasiljevic A., Mercier S., Roume J., Trestard L.,
RA Saugier-Veber P., Cordier M.P., Layet V., Legendre M.,
RA Vigouroux-Castera A., Lunardi J., Bayes M., Jouk P.S., Rigonnot L.,
RA Granier M., Sternberg D., Warszawski J., Gut I., Gonzales M., Tawk M.,
RA Melki J.;
RT "Mutations in CNTNAP1 and ADCY6 are responsible for severe arthrogryposis
RT multiplex congenita with axoglial defects.";
RL Hum. Mol. Genet. 23:2279-2289(2014).
RN [3]
RP VARIANTS LCCS7 ARG-323 AND 623-TRP--GLU-1384 DEL.
RX PubMed=27782105; DOI=10.1038/ejhg.2016.142;
RA Nizon M., Cogne B., Vallat J.M., Joubert M., Liet J.M., Simon L.,
RA Vincent M., Kuery S., Boisseau P., Schmitt S., Mercier S., Beneteau C.,
RA Larrose C., Coste M., Latypova X., Pereon Y., Mussini J.M., Bezieau S.,
RA Isidor B.;
RT "Two novel variants in CNTNAP1 in two siblings presenting with congenital
RT hypotonia and hypomyelinating neuropathy.";
RL Eur. J. Hum. Genet. 25:150-152(2016).
RN [4]
RP INVOLVEMENT IN CHN3, VARIANTS CHN3 623-TRP--GLU-1384 DEL; 671-GLN--GLU-1384
RP DEL AND CYS-764, AND FUNCTION.
RX PubMed=27818385; DOI=10.1093/jnen/nlw093;
RA Vallat J.M., Nizon M., Magee A., Isidor B., Magy L., Pereon Y., Richard L.,
RA Ouvrier R., Cogne B., Devaux J., Zuchner S., Mathis S.;
RT "Contactin-Associated Protein 1 (CNTNAP1) Mutations Induce Characteristic
RT Lesions of the Paranodal Region.";
RL J. Neuropathol. Exp. Neurol. 75:1155-1159(2016).
RN [5]
RP INVOLVEMENT IN LCCS7.
RX PubMed=28254648; DOI=10.1016/j.ejmg.2017.02.006;
RA Lakhani S., Doan R., Almureikhi M., Partlow J.N., Al Saffar M.,
RA Elsaid M.F., Alaaraj N., James Barkovich A., Walsh C.A., Ben-Omran T.;
RT "Identification of a novel CNTNAP1 mutation causing arthrogryposis
RT multiplex congenita with cerebral and cerebellar atrophy.";
RL Eur. J. Med. Genet. 60:245-249(2017).
RN [6]
RP INVOLVEMENT IN CHN3, AND CHN3 VARIANT PRO-388.
RX PubMed=27668699; DOI=10.1002/mus.25416;
RA Mehta P., Kuespert M., Bale T., Brownstein C.A., Towne M.C.,
RA De Girolami U., Shi J., Beggs A.H., Darras B.T., Wegner M., Piao X.,
RA Agrawal P.B.;
RT "Novel mutation in CNTNAP1 results in congenital hypomyelinating
RT neuropathy.";
RL Muscle Nerve 55:761-765(2017).
RN [7]
RP VARIANT LCCS7 672-TRP--GLU-1384 DEL, VARIANTS CHN3 671-GLN--GLU-1384 DEL
RP AND CYS-764, AND FUNCTION.
RX PubMed=28374019; DOI=10.1212/nxg.0000000000000144;
RA Hengel H., Magee A., Mahanjah M., Vallat J.M., Ouvrier R., Abu-Rashid M.,
RA Mahamid J., Schuele R., Schulze M., Kraegeloh-Mann I., Bauer P.,
RA Zuechner S., Sharkia R., Schoels L.;
RT "CNTNAP1 mutations cause CNS hypomyelination and neuropathy with or without
RT arthrogryposis.";
RL Neurol. Genet. 3:E144-E144(2017).
RN [8]
RP INVOLVEMENT IN CHN3, AND VARIANTS CHN3 GLN-50; PRO-212; 559-TRP--GLU-1384
RP DEL; 621-ARG--GLU-1384 DEL; PRO-714; 782-ARG--GLU-1384 DEL AND
RP 896-TRP--GLU-1384 DEL.
RX PubMed=29511323; DOI=10.1038/s41431-018-0110-x;
RA Low K.J., Stals K., Caswell R., Wakeling M., Clayton-Smith J.,
RA Donaldson A., Foulds N., Norman A., Splitt M., Urankar K., Vijayakumar K.,
RA Majumdar A., Study D., Ellard S., Smithson S.F.;
RT "Phenotype of CNTNAP1: a study of patients demonstrating a specific severe
RT congenital hypomyelinating neuropathy with survival beyond infancy.";
RL Eur. J. Hum. Genet. 26:796-807(2018).
CC -!- FUNCTION: Required, with CNTNAP2, for radial and longitudinal
CC organization of myelinated axons. Plays a role in the formation of
CC functional distinct domains critical for saltatory conduction of nerve
CC impulses in myelinated nerve fibers. Demarcates the paranodal region of
CC the axo-glial junction. In association with contactin involved in the
CC signaling between axons and myelinating glial cells.
CC {ECO:0000269|PubMed:24319099, ECO:0000269|PubMed:27818385,
CC ECO:0000269|PubMed:28374019}.
CC -!- SUBUNIT: Interacts with CNTN1/contactin in cis form.
CC {ECO:0000269|PubMed:9118959}.
CC -!- INTERACTION:
CC P78357; P16333: NCK1; NbExp=2; IntAct=EBI-1751903, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, paranodal septate
CC junction {ECO:0000250|UniProtKB:O54991}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Weak expression
CC detected in ovary, pancreas, colon, lung, heart, intestine and testis.
CC -!- DISEASE: Lethal congenital contracture syndrome 7 (LCCS7) [MIM:616286]:
CC A form of lethal congenital contracture syndrome, an autosomal
CC recessive disorder characterized by degeneration of anterior horn
CC neurons, extreme skeletal muscle atrophy and congenital non-progressive
CC joint contractures. The contractures can involve the upper or lower
CC limbs and/or the vertebral column, leading to various degrees of
CC flexion or extension limitations evident at birth. LCCS7 is a severe
CC axoglial disease characterized by congenital distal joint contractures,
CC polyhydramnios, reduced fetal movements, and motor paralysis leading to
CC death early in the neonatal period. {ECO:0000269|PubMed:24319099,
CC ECO:0000269|PubMed:27782105, ECO:0000269|PubMed:28254648,
CC ECO:0000269|PubMed:28374019}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Neuropathy, congenital hypomyelinating, 3 (CHN3) [MIM:618186]:
CC A form of congenital hypomyelinating neuropathy, a neurologic disorder
CC characterized by early-onset hypotonia, areflexia, distal muscle
CC weakness, and very slow nerve conduction velocities (NCV) resulting
CC from improper myelination of axons. In its extreme form, it may present
CC with severe joint contractures or arthrogryposis multiplex congenita
CC and respiratory insufficiency. In less severe cases patients may
CC achieve walking. Patients lack both active myelin breakdown and well-
CC organized onion bulbs on sural nerve biopsies, have absence of
CC inflammation, and show hypomyelination of most or all fibers. CHN3 is a
CC severe autosomal recessive form characterized by onset of neurogenic
CC muscle impairment in utero. Affected individuals have profoundly
CC impaired psychomotor development and may die in infancy or early
CC childhood. {ECO:0000269|PubMed:27668699, ECO:0000269|PubMed:27818385,
CC ECO:0000269|PubMed:28374019, ECO:0000269|PubMed:29511323}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; U87223; AAB48481.1; -; mRNA.
DR CCDS; CCDS11436.1; -.
DR RefSeq; NP_003623.1; NM_003632.2.
DR RefSeq; XP_016880727.1; XM_017025238.1.
DR AlphaFoldDB; P78357; -.
DR SMR; P78357; -.
DR BioGRID; 114078; 100.
DR CORUM; P78357; -.
DR IntAct; P78357; 22.
DR MINT; P78357; -.
DR STRING; 9606.ENSP00000264638; -.
DR GlyGen; P78357; 17 sites.
DR iPTMnet; P78357; -.
DR PhosphoSitePlus; P78357; -.
DR BioMuta; CNTNAP1; -.
DR DMDM; 17433016; -.
DR EPD; P78357; -.
DR jPOST; P78357; -.
DR MassIVE; P78357; -.
DR MaxQB; P78357; -.
DR PaxDb; P78357; -.
DR PeptideAtlas; P78357; -.
DR PRIDE; P78357; -.
DR ProteomicsDB; 57588; -.
DR ABCD; P78357; 1 sequenced antibody.
DR Antibodypedia; 2336; 240 antibodies from 35 providers.
DR DNASU; 8506; -.
DR Ensembl; ENST00000264638.9; ENSP00000264638.3; ENSG00000108797.12.
DR GeneID; 8506; -.
DR KEGG; hsa:8506; -.
DR MANE-Select; ENST00000264638.9; ENSP00000264638.3; NM_003632.3; NP_003623.1.
DR UCSC; uc002iay.4; human.
DR CTD; 8506; -.
DR DisGeNET; 8506; -.
DR GeneCards; CNTNAP1; -.
DR GeneReviews; CNTNAP1; -.
DR HGNC; HGNC:8011; CNTNAP1.
DR HPA; ENSG00000108797; Tissue enhanced (brain).
DR MalaCards; CNTNAP1; -.
DR MIM; 602346; gene.
DR MIM; 616286; phenotype.
DR MIM; 618186; phenotype.
DR neXtProt; NX_P78357; -.
DR OpenTargets; ENSG00000108797; -.
DR Orphanet; 2680; Hypomyelination neuropathy-arthrogryposis syndrome.
DR PharmGKB; PA26691; -.
DR VEuPathDB; HostDB:ENSG00000108797; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000160825; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; P78357; -.
DR OMA; HCAHPRF; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; P78357; -.
DR TreeFam; TF321823; -.
DR PathwayCommons; P78357; -.
DR Reactome; R-HSA-447043; Neurofascin interactions.
DR SignaLink; P78357; -.
DR BioGRID-ORCS; 8506; 28 hits in 1082 CRISPR screens.
DR ChiTaRS; CNTNAP1; human.
DR GenomeRNAi; 8506; -.
DR Pharos; P78357; Tbio.
DR PRO; PR:P78357; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P78357; protein.
DR Bgee; ENSG00000108797; Expressed in right hemisphere of cerebellum and 134 other tissues.
DR ExpressionAtlas; P78357; baseline and differential.
DR Genevisible; P78357; HS.
DR GO; GO:0016021; C:integral component of membrane; ISS:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0033270; C:paranode region of axon; ISS:BHF-UCL.
DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:BHF-UCL.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
DR GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0019227; P:neuronal action potential propagation; ISS:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; IMP:UniProtKB.
DR GO; GO:1990227; P:paranodal junction maintenance; IEA:Ensembl.
DR GO; GO:0097106; P:postsynaptic density organization; IEA:Ensembl.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:UniProtKB.
DR GO; GO:0002175; P:protein localization to paranode region of axon; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR028872; Caspr1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF43; PTHR15036:SF43; 3.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 4.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Disease variant; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Neuropathy; Phosphoprotein;
KW Reference proteome; Repeat; SH3-binding; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1384
FT /note="Contactin-associated protein 1"
FT /id="PRO_0000019503"
FT TOPO_DOM 20..1283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1284..1304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1305..1384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..168
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 203..355
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 389..538
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 540..577
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 576..795
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 813..956
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 957..996
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1088..1250
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1319..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1328..1369
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1350..1370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54991"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1078
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..168
FT /evidence="ECO:0000250"
FT DISULFID 323..355
FT /evidence="ECO:0000250"
FT DISULFID 506..538
FT /evidence="ECO:0000250"
FT DISULFID 544..555
FT /evidence="ECO:0000250"
FT DISULFID 549..564
FT /evidence="ECO:0000250"
FT DISULFID 566..576
FT /evidence="ECO:0000250"
FT DISULFID 930..957
FT /evidence="ECO:0000250"
FT DISULFID 961..974
FT /evidence="ECO:0000250"
FT DISULFID 968..983
FT /evidence="ECO:0000250"
FT DISULFID 985..995
FT /evidence="ECO:0000250"
FT DISULFID 1209..1250
FT /evidence="ECO:0000250"
FT VARIANT 50
FT /note="P -> Q (in CHN3)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081766"
FT VARIANT 212
FT /note="L -> P (in CHN3; dbSNP:rs1567969825)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081767"
FT VARIANT 323
FT /note="C -> R (in LCCS7; dbSNP:rs768554986)"
FT /evidence="ECO:0000269|PubMed:27782105"
FT /id="VAR_078818"
FT VARIANT 388
FT /note="R -> P (in CHN3; dbSNP:rs779027563)"
FT /evidence="ECO:0000269|PubMed:27668699"
FT /id="VAR_078819"
FT VARIANT 522
FT /note="V -> L (in dbSNP:rs35437096)"
FT /id="VAR_050267"
FT VARIANT 559..1384
FT /note="Missing (in CHN3)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081768"
FT VARIANT 621..1384
FT /note="Missing (in CHN3)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081769"
FT VARIANT 623..1384
FT /note="Missing (in LCCS7 and CHN3)"
FT /evidence="ECO:0000269|PubMed:27782105,
FT ECO:0000269|PubMed:27818385"
FT /id="VAR_078820"
FT VARIANT 671..1384
FT /note="Missing (in CHN3)"
FT /evidence="ECO:0000269|PubMed:27818385,
FT ECO:0000269|PubMed:28374019"
FT /id="VAR_078821"
FT VARIANT 672..1384
FT /note="Missing (in LCCS7)"
FT /evidence="ECO:0000269|PubMed:28374019"
FT /id="VAR_078822"
FT VARIANT 714
FT /note="R -> P (in CHN3)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081770"
FT VARIANT 764
FT /note="R -> C (in CHN3; dbSNP:rs761805324)"
FT /evidence="ECO:0000269|PubMed:27818385,
FT ECO:0000269|PubMed:28374019"
FT /id="VAR_078823"
FT VARIANT 782..1384
FT /note="Missing (in CHN3)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081771"
FT VARIANT 896..1384
FT /note="Missing (in CHN3)"
FT /evidence="ECO:0000269|PubMed:29511323"
FT /id="VAR_081772"
SQ SEQUENCE 1384 AA; 156267 MW; 7727A13DF626DDCA CRC64;
MMHLRLFCIL LAAVSGAEGW GYYGCDEELV GPLYARSLGA SSYYSLLTAP RFARLHGISG
WSPRIGDPNP WLQIDLMKKH RIRAVATQGS FNSWDWVTRY MLLYGDRVDS WTPFYQRGHN
STFFGNVNES AVVRHDLHFH FTARYIRIVP LAWNPRGKIG LRLGLYGCPY KADILYFDGD
DAISYRFPRG VSRSLWDVFA FSFKTEEKDG LLLHAEGAQG DYVTLELEGA HLLLHMSLGS
SPIQPRPGHT TVSAGGVLND QHWHYVRVDR FGRDVNFTLD GYVQRFILNG DFERLNLDTE
MFIGGLVGAA RKNLAYRHNF RGCIENVIFN RVNIADLAVR RHSRITFEGK VAFRCLDPVP
HPINFGGPHN FVQVPGFPRR GRLAVSFRFR TWDLTGLLLF SRLGDGLGHV ELTLSEGQVN
VSIAQSGRKK LQFAAGYRLN DGFWHEVNFV AQENHAVISI DDVEGAEVRV SYPLLIRTGT
SYFFGGCPKP ASRWDCHSNQ TAFHGCMELL KVDGQLVNLT LVEGRRLGFY AEVLFDTCGI
TDRCSPNMCE HDGRCYQSWD DFICYCELTG YKGETCHTPL YKESCEAYRL SGKTSGNFTI
DPDGSGPLKP FVVYCDIREN RAWTVVRHDR LWTTRVTGSS MERPFLGAIQ YWNASWEEVS
ALANASQHCE QWIEFSCYNS RLLNTAGGYP YSFWIGRNEE QHFYWGGSQP GIQRCACGLD
RSCVDPALYC NCDADQPQWR TDKGLLTFVD HLPVTQVVIG DTNRSTSEAQ FFLRPLRCYG
DRNSWNTISF HTGAALRFPP IRANHSLDVS FYFRTSAPSG VFLENMGGPY CQWRRPYVRV
ELNTSRDVVF AFDVGNGDEN LTVHSDDFEF NDDEWHLVRA EINVKQARLR VDHRPWVLRP
MPLQTYIWME YDQPLYVGSA ELKRRPFVGC LRAMRLNGVT LNLEGRANAS EGTSPNCTGH
CAHPRLPCFH GGRCVERYSY YTCDCDLTAF DGPYCNHDIG GFFEPGTWMR YNLQSALRSA
AREFSHMLSR PVPGYEPGYI PGYDTPGYVP GYHGPGYRLP DYPRPGRPVP GYRGPVYNVT
GEEVSFSFST SSAPAVLLYV SSFVRDYMAV LIKDDGTLQL RYQLGTSPYV YQLTTRPVTD
GQPHSINITR VYRNLFIQVD YFPLTEQKFS LLVDSQLDSP KALYLGRVME TGVIDPEIQR
YNTPGFSGCL SGVRFNNVAP LKTHFRTPRP MTAELAEALR VQGELSESNC GAMPRLVSEV
PPELDPWYLP PDFPYYHDEG WVAILLGFLV AFLLLGLVGM LVLFYLQNHR YKGSYHTNEP
KAAHEYHPGS KPPLPTSGPA QVPTPTAAPN QAPASAPAPA PTPAPAPGPR DQNLPQILEE
SRSE
