ID   CHRD_HUMAN              Reviewed;         955 AA.
AC   Q9H2X0; O95254; Q2M1I8; Q6UW83; Q9H2D3; Q9H2W8; Q9H2W9; Q9P0Z2; Q9P0Z3;
AC   Q9P0Z4; Q9P0Z5;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Chordin;
DE   Flags: Precursor;
GN   Name=CHRD; ORFNames=UNQ217/PRO243;
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] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT LEU-630.
RX   PubMed=11472837; DOI=10.1016/s0925-4773(01)00423-3;
RA   Millet C., Lemaire P., Orsetti B., Guglielmi P., Francois V.;
RT   "The human chordin gene encodes several differentially expressed spliced
RT   variants with distinct BMP opposing activities.";
RL   Mech. Dev. 106:85-96(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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] (ISOFORM 1).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 115-955 (ISOFORM 5), AND VARIANT LEU-630.
RX   PubMed=9782094; DOI=10.1006/geno.1998.5474;
RA   Pappano W.N., Scott I.C., Clark T.G., Eddy R.L., Shows T.B.,
RA   Greenspan D.S.;
RT   "Coding sequence and expression patterns of mouse chordin and mapping of
RT   the cognate mouse chrd and human CHRD genes.";
RL   Genomics 52:236-239(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-125; 705-762; 784-850 AND 872-932.
RX   PubMed=10648240; DOI=10.1242/dev.127.4.821;
RA   Larrain J., Bachiller D., Lu B., Agius E., Piccolo S., De Robertis E.M.;
RT   "BMP-binding modules in chordin: a model for signalling regulation in the
RT   extracellular space.";
RL   Development 127:821-830(2000).
RN   [6]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
CC   -!- FUNCTION: Dorsalizing factor. Key developmental protein that dorsalizes
CC       early vertebrate embryonic tissues by binding to ventralizing TGF-beta
CC       family bone morphogenetic proteins (BMPs) and sequestering them in
CC       latent complexes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TWSG1 and/or BMP4. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9H2X0; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-947551, EBI-10173507;
CC       Q9H2X0; P13497: BMP1; NbExp=2; IntAct=EBI-947551, EBI-489827;
CC       Q9H2X0; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-947551, EBI-744545;
CC       Q9H2X0; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-947551, EBI-12593838;
CC       Q9H2X0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-947551, EBI-3867333;
CC       Q9H2X0; P15976-2: GATA1; NbExp=3; IntAct=EBI-947551, EBI-9090198;
CC       Q9H2X0; P49639: HOXA1; NbExp=4; IntAct=EBI-947551, EBI-740785;
CC       Q9H2X0; Q0VD86: INCA1; NbExp=3; IntAct=EBI-947551, EBI-6509505;
CC       Q9H2X0; O76011: KRT34; NbExp=3; IntAct=EBI-947551, EBI-1047093;
CC       Q9H2X0; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-947551, EBI-11959885;
CC       Q9H2X0; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-947551, EBI-11749135;
CC       Q9H2X0; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-947551, EBI-10172150;
CC       Q9H2X0; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-947551, EBI-10172290;
CC       Q9H2X0; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-947551, EBI-10171774;
CC       Q9H2X0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-947551, EBI-10172052;
CC       Q9H2X0; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-947551, EBI-10210845;
CC       Q9H2X0; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-947551, EBI-10176379;
CC       Q9H2X0; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-947551, EBI-11953334;
CC       Q9H2X0; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-947551, EBI-12196745;
CC       Q9H2X0; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-947551, EBI-1048945;
CC       Q9H2X0; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-947551, EBI-739863;
CC       Q9H2X0; Q9BYR5: KRTAP4-2; NbExp=6; IntAct=EBI-947551, EBI-10172511;
CC       Q9H2X0; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-947551, EBI-3958099;
CC       Q9H2X0; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-947551, EBI-1044640;
CC       Q9H2X0; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-947551, EBI-1043191;
CC       Q9H2X0; Q5T751: LCE1C; NbExp=3; IntAct=EBI-947551, EBI-12224199;
CC       Q9H2X0; Q5T754: LCE1F; NbExp=3; IntAct=EBI-947551, EBI-11958008;
CC       Q9H2X0; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-947551, EBI-11955689;
CC       Q9H2X0; O14910: LIN7A; NbExp=3; IntAct=EBI-947551, EBI-2513988;
CC       Q9H2X0; P50222: MEOX2; NbExp=3; IntAct=EBI-947551, EBI-748397;
CC       Q9H2X0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-947551, EBI-16439278;
CC       Q9H2X0; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-947551, EBI-945833;
CC       Q9H2X0; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-947551, EBI-22310682;
CC       Q9H2X0; Q92570: NR4A3; NbExp=3; IntAct=EBI-947551, EBI-13644623;
CC       Q9H2X0; P32242: OTX1; NbExp=3; IntAct=EBI-947551, EBI-740446;
CC       Q9H2X0; O15162: PLSCR1; NbExp=3; IntAct=EBI-947551, EBI-740019;
CC       Q9H2X0; Q12837: POU4F2; NbExp=3; IntAct=EBI-947551, EBI-17236143;
CC       Q9H2X0; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-947551, EBI-3918154;
CC       Q9H2X0; Q16348: SLC15A2; NbExp=3; IntAct=EBI-947551, EBI-12806032;
CC       Q9H2X0; P84022: SMAD3; NbExp=2; IntAct=EBI-947551, EBI-347161;
CC       Q9H2X0; O43609: SPRY1; NbExp=3; IntAct=EBI-947551, EBI-3866665;
CC       Q9H2X0; O43597: SPRY2; NbExp=3; IntAct=EBI-947551, EBI-742487;
CC       Q9H2X0; O43610: SPRY3; NbExp=3; IntAct=EBI-947551, EBI-12290641;
CC       Q9H2X0; Q8IWZ5: TRIM42; NbExp=5; IntAct=EBI-947551, EBI-5235829;
CC       Q9H2X0; O14817: TSPAN4; NbExp=3; IntAct=EBI-947551, EBI-8652667;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=Q9H2X0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H2X0-2; Sequence=VSP_001069, VSP_001070;
CC       Name=3;
CC         IsoId=Q9H2X0-3; Sequence=VSP_001071, VSP_001072;
CC       Name=4;
CC         IsoId=Q9H2X0-4; Sequence=VSP_001073, VSP_001074;
CC       Name=5;
CC         IsoId=Q9H2X0-5; Sequence=VSP_001075;
CC   -!- TISSUE SPECIFICITY: Expressed at the highest level in liver.
CC   -!- PTM: Cleaved by tolloid proteases; cleavage participates in
CC       dorsoventral patterning during early development. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the chordin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF209928; AAG35767.1; -; mRNA.
DR   EMBL; AF209929; AAG35768.1; -; mRNA.
DR   EMBL; AF209930; AAG35769.1; -; mRNA.
DR   EMBL; AF283325; AAG35784.1; -; mRNA.
DR   EMBL; AY358926; AAQ89285.1; -; mRNA.
DR   EMBL; BC112345; AAI12346.1; -; mRNA.
DR   EMBL; AF076612; AAC69835.1; -; mRNA.
DR   EMBL; AF136632; AAF70236.1; -; Genomic_DNA.
DR   EMBL; AF136633; AAF70237.1; -; Genomic_DNA.
DR   EMBL; AF136634; AAF70238.1; -; Genomic_DNA.
DR   EMBL; AF136635; AAF70239.1; -; Genomic_DNA.
DR   CCDS; CCDS3266.1; -. [Q9H2X0-1]
DR   RefSeq; NP_001291401.1; NM_001304472.1.
DR   RefSeq; NP_001291402.1; NM_001304473.1.
DR   RefSeq; NP_001291403.1; NM_001304474.1.
DR   RefSeq; NP_003732.2; NM_003741.3. [Q9H2X0-1]
DR   AlphaFoldDB; Q9H2X0; -.
DR   SMR; Q9H2X0; -.
DR   BioGRID; 114198; 122.
DR   DIP; DIP-48857N; -.
DR   IntAct; Q9H2X0; 57.
DR   MINT; Q9H2X0; -.
DR   STRING; 9606.ENSP00000204604; -.
DR   GlyCosmos; Q9H2X0; 4 sites, No reported glycans.
DR   GlyGen; Q9H2X0; 4 sites.
DR   iPTMnet; Q9H2X0; -.
DR   PhosphoSitePlus; Q9H2X0; -.
DR   BioMuta; CHRD; -.
DR   DMDM; 118572631; -.
DR   jPOST; Q9H2X0; -.
DR   MassIVE; Q9H2X0; -.
DR   PaxDb; 9606-ENSP00000204604; -.
DR   PeptideAtlas; Q9H2X0; -.
DR   ProteomicsDB; 80611; -. [Q9H2X0-1]
DR   ProteomicsDB; 80612; -. [Q9H2X0-2]
DR   ProteomicsDB; 80613; -. [Q9H2X0-3]
DR   ProteomicsDB; 80614; -. [Q9H2X0-4]
DR   ProteomicsDB; 80615; -. [Q9H2X0-5]
DR   Antibodypedia; 33823; 284 antibodies from 27 providers.
DR   DNASU; 8646; -.
DR   Ensembl; ENST00000204604.6; ENSP00000204604.1; ENSG00000090539.16. [Q9H2X0-1]
DR   Ensembl; ENST00000348986.3; ENSP00000334036.4; ENSG00000090539.16. [Q9H2X0-5]
DR   Ensembl; ENST00000356534.7; ENSP00000348930.3; ENSG00000090539.16. [Q9H2X0-2]
DR   Ensembl; ENST00000420973.5; ENSP00000392794.1; ENSG00000090539.16. [Q9H2X0-4]
DR   Ensembl; ENST00000448472.5; ENSP00000408624.1; ENSG00000090539.16. [Q9H2X0-3]
DR   GeneID; 8646; -.
DR   KEGG; hsa:8646; -.
DR   MANE-Select; ENST00000204604.6; ENSP00000204604.1; NM_003741.4; NP_003732.2.
DR   UCSC; uc003fov.3; human. [Q9H2X0-1]
DR   AGR; HGNC:1949; -.
DR   CTD; 8646; -.
DR   DisGeNET; 8646; -.
DR   GeneCards; CHRD; -.
DR   HGNC; HGNC:1949; CHRD.
DR   HPA; ENSG00000090539; Tissue enhanced (brain, liver).
DR   MIM; 603475; gene.
DR   neXtProt; NX_Q9H2X0; -.
DR   OpenTargets; ENSG00000090539; -.
DR   PharmGKB; PA26482; -.
DR   VEuPathDB; HostDB:ENSG00000090539; -.
DR   eggNOG; ENOG502QR4J; Eukaryota.
DR   GeneTree; ENSGT00940000161767; -.
DR   HOGENOM; CLU_2497257_0_0_1; -.
DR   InParanoid; Q9H2X0; -.
DR   OMA; CCKSCPG; -.
DR   OrthoDB; 3039493at2759; -.
DR   PhylomeDB; Q9H2X0; -.
DR   TreeFam; TF106451; -.
DR   PathwayCommons; Q9H2X0; -.
DR   SignaLink; Q9H2X0; -.
DR   BioGRID-ORCS; 8646; 17 hits in 1146 CRISPR screens.
DR   GenomeRNAi; 8646; -.
DR   Pharos; Q9H2X0; Tbio.
DR   PRO; PR:Q9H2X0; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9H2X0; Protein.
DR   Bgee; ENSG00000090539; Expressed in right lobe of liver and 117 other cell types or tissues.
DR   ExpressionAtlas; Q9H2X0; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0036122; F:BMP binding; IBA:GO_Central.
DR   GO; GO:0019955; F:cytokine binding; NAS:BHF-UCL.
DR   GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR   GO; GO:0033504; P:floor plate development; TAS:BHF-UCL.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0001501; P:skeletal system development; TAS:UniProtKB.
DR   GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:BHF-UCL.
DR   Gene3D; 6.20.200.20; -; 1.
DR   InterPro; IPR016353; Chordin.
DR   InterPro; IPR010895; CHRD.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR46526; CHORDIN; 1.
DR   PANTHER; PTHR46526:SF1; CHORDIN; 1.
DR   Pfam; PF07452; CHRD; 3.
DR   Pfam; PF00093; VWC; 3.
DR   PIRSF; PIRSF002496; Chordin; 1.
DR   SMART; SM00754; CHRD; 4.
DR   SMART; SM00214; VWC; 4.
DR   SUPFAM; SSF57603; FnI-like domain; 4.
DR   PROSITE; PS50933; CHRD; 4.
DR   PROSITE; PS01208; VWFC_1; 2.
DR   PROSITE; PS50184; VWFC_2; 2.
DR   Genevisible; Q9H2X0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..955
FT                   /note="Chordin"
FT                   /id="PRO_0000005364"
FT   DOMAIN          49..126
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          168..277
FT                   /note="CHRD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          279..402
FT                   /note="CHRD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          403..524
FT                   /note="CHRD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          530..650
FT                   /note="CHRD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          703..763
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          784..850
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          872..932
FT                   /note="VWFC 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REGION          124..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..697
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         85..94
FT                   /note="PQWGRRTRGP -> TGTLRPREMK (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11472837"
FT                   /id="VSP_001071"
FT   VAR_SEQ         85..86
FT                   /note="PQ -> GP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11472837"
FT                   /id="VSP_001069"
FT   VAR_SEQ         87..955
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11472837"
FT                   /id="VSP_001070"
FT   VAR_SEQ         95..955
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11472837"
FT                   /id="VSP_001072"
FT   VAR_SEQ         328..350
FT                   /note="GLTQVPLRLQILHQGQLLRELQA -> DSTPGAATARTSGQCLSPGTRLC
FT                   (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11472837"
FT                   /id="VSP_001073"
FT   VAR_SEQ         351..955
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11472837"
FT                   /id="VSP_001074"
FT   VAR_SEQ         441..480
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:9782094"
FT                   /id="VSP_001075"
FT   VARIANT         94
FT                   /note="P -> S (in dbSNP:rs34095724)"
FT                   /id="VAR_048727"
FT   VARIANT         630
FT                   /note="M -> L (in dbSNP:rs16858780)"
FT                   /evidence="ECO:0000269|PubMed:11472837,
FT                   ECO:0000269|PubMed:9782094"
FT                   /id="VAR_021517"
FT   CONFLICT        70
FT                   /note="E -> Q (in Ref. 2; AAQ89285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115..118
FT                   /note="RQLP -> QVAA (in Ref. 4; AAC69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="V -> A (in Ref. 4; AAC69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="S -> P (in Ref. 4; AAC69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        674
FT                   /note="T -> P (in Ref. 4; AAC69835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        939
FT                   /note="Missing (in Ref. 2; AAQ89285)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   955 AA;  102032 MW;  53F9D9F39A517686 CRC64;
     MPSLPAPPAP LLLLGLLLLG SRPARGAGPE PPVLPIRSEK EPLPVRGAAG CTFGGKVYAL
     DETWHPDLGE PFGVMRCVLC ACEAPQWGRR TRGPGRVSCK NIKPECPTPA CGQPRQLPGH
     CCQTCPQERS SSERQPSGLS FEYPRDPEHR SYSDRGEPGA EERARGDGHT DFVALLTGPR
     SQAVARARVS LLRSSLRFSI SYRRLDRPTR IRFSDSNGSV LFEHPAAPTQ DGLVCGVWRA
     VPRLSLRLLR AEQLHVALVT LTHPSGEVWG PLIRHRALAA ETFSAILTLE GPPQQGVGGI
     TLLTLSDTED SLHFLLLFRG LLEPRSGGLT QVPLRLQILH QGQLLRELQA NVSAQEPGFA
     EVLPNLTVQE MDWLVLGELQ MALEWAGRPG LRISGHIAAR KSCDVLQSVL CGADALIPVQ
     TGAAGSASLT LLGNGSLIYQ VQVVGTSSEV VAMTLETKPQ RRDQRTVLCH MAGLQPGGHT
     AVGICPGLGA RGAHMLLQNE LFLNVGTKDF PDGELRGHVA ALPYCGHSAR HDTLPVPLAG
     ALVLPPVKSQ AAGHAWLSLD THCHLHYEVL LAGLGGSEQG TVTAHLLGPP GTPGPRRLLK
     GFYGSEAQGV VKDLEPELLR HLAKGMASLM ITTKGSPRGE LRGQVHIANQ CEVGGLRLEA
     AGAEGVRALG APDTASAAPP VVPGLPALAP AKPGGPGRPR DPNTCFFEGQ QRPHGARWAP
     NYDPLCSLCT CQRRTVICDP VVCPPPSCPH PVQAPDQCCP VCPEKQDVRD LPGLPRSRDP
     GEGCYFDGDR SWRAAGTRWH PVVPPFGLIK CAVCTCKGGT GEVHCEKVQC PRLACAQPVR
     VNPTDCCKQC PVGSGAHPQL GDPMQADGPR GCRFAGQWFP ESQSWHPSVP PFGEMSCITC
     RCGAGVPHCE RDDCSLPLSC GSGKESRCCS RCTAHRRPAP ETRTDPELEK EAEGS
//