ID   CRDL1_HUMAN             Reviewed;         456 AA.
AC   Q9BU40; B1AKD0; B4DMP3; D3DUY6; E9PGS5; Q539E4; Q9Y3H7;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 2.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=Chordin-like protein 1;
DE   AltName: Full=Neuralin-1;
DE   AltName: Full=Neurogenesin-1;
DE   AltName: Full=Ventroptin;
DE   Flags: Precursor;
GN   Name=CHRDL1; Synonyms=NRLN1;
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 3), FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   PubMed=18587495;
RA   Kane R., Godson C., O'Brien C.;
RT   "Chordin-like 1, a bone morphogenetic protein-4 antagonist, is upregulated
RT   by hypoxia in human retinal pericytes and plays a role in regulating
RT   angiogenesis.";
RL   Mol. Vis. 14:1138-1148(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   TISSUE=Astrocyte, Brain, and Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND VARIANT MGC1 PHE-260.
RX   PubMed=22284829; DOI=10.1016/j.ajhg.2011.12.019;
RA   Webb T.R., Matarin M., Gardner J.C., Kelberman D., Hassan H., Ang W.,
RA   Michaelides M., Ruddle J.B., Pennell C.E., Yazar S., Khor C.C., Aung T.,
RA   Yogarajah M., Robson A.G., Holder G.E., Cheetham M.E., Traboulsi E.I.,
RA   Moore A.T., Sowden J.C., Sisodiya S.M., Mackey D.A., Tuft S.J.,
RA   Hardcastle A.J.;
RT   "X-linked megalocornea caused by mutations in CHRDL1 identifies an
RT   essential role for ventroptin in anterior segment development.";
RL   Am. J. Hum. Genet. 90:247-259(2012).
CC   -!- FUNCTION: Antagonizes the function of BMP4 by binding to it and
CC       preventing its interaction with receptors. Alters the fate commitment
CC       of neural stem cells from gliogenesis to neurogenesis. Contributes to
CC       neuronal differentiation of neural stem cells in the brain by
CC       preventing the adoption of a glial fate. May play a crucial role in
CC       dorsoventral axis formation. May play a role in embryonic bone
CC       formation (By similarity). May also play an important role in
CC       regulating retinal angiogenesis through modulation of BMP4 actions in
CC       endothelial cells. Plays a role during anterior segment eye
CC       development. {ECO:0000250, ECO:0000269|PubMed:18587495,
CC       ECO:0000269|PubMed:22284829}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9BU40-6; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BU40-3; Sequence=VSP_060079, VSP_060080;
CC       Name=3;
CC         IsoId=Q9BU40-4; Sequence=VSP_060078, VSP_060080;
CC       Name=4;
CC         IsoId=Q9BU40-5; Sequence=VSP_060080;
CC   -!- TISSUE SPECIFICITY: Expressed in the developing cornea and in the eye
CC       anterior segment in addition to the retina. Differentially expressed in
CC       the fetal brain. There is high expression in cerebellum and neocortex.
CC       Expressed in retinal pericytes. {ECO:0000269|PubMed:18587495,
CC       ECO:0000269|PubMed:22284829}.
CC   -!- INDUCTION: By hypoxia in retinal pericytes.
CC       {ECO:0000269|PubMed:18587495}.
CC   -!- DISEASE: Megalocornea 1, X-linked (MGC1) [MIM:309300]: An eye disorder
CC       in which the corneal diameter is bilaterally enlarged (greater than 13
CC       mm) without an increase in intraocular pressure. It may also be
CC       referred to as anterior megalophthalmos, since the entire anterior
CC       segment is larger than normal. Features of megalocornea in addition to
CC       a deep anterior chamber include astigmatic refractive errors, atrophy
CC       of the iris stroma, miosis secondary to decreased function of the
CC       dilator muscle, iridodonesis, and tremulousness, subluxation, or
CC       dislocation of the lens. Whereas most affected individuals exhibit
CC       normal ocular function, complications include cataract development and
CC       glaucoma following lenticular dislocation or subluxation.
CC       {ECO:0000269|PubMed:22284829}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AY608914; AAU25841.1; -; mRNA.
DR   EMBL; AK293106; BAF85795.1; -; mRNA.
DR   EMBL; AK297563; BAG59955.1; -; mRNA.
DR   EMBL; AK312270; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL049176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL591489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471120; EAX02656.1; -; Genomic_DNA.
DR   EMBL; CH471120; EAX02657.1; -; Genomic_DNA.
DR   EMBL; BC002909; AAH02909.2; -; mRNA.
DR   CCDS; CCDS14553.1; -. [Q9BU40-6]
DR   CCDS; CCDS48148.2; -. [Q9BU40-3]
DR   CCDS; CCDS48149.1; -. [Q9BU40-4]
DR   CCDS; CCDS48150.1; -. [Q9BU40-5]
DR   RefSeq; NP_001137453.1; NM_001143981.1. [Q9BU40-4]
DR   RefSeq; NP_001137454.1; NM_001143982.1. [Q9BU40-5]
DR   RefSeq; NP_001137455.2; NM_001143983.2. [Q9BU40-3]
DR   RefSeq; NP_660277.2; NM_145234.3. [Q9BU40-6]
DR   RefSeq; XP_005262278.1; XM_005262221.1.
DR   RefSeq; XP_005262279.1; XM_005262222.3. [Q9BU40-5]
DR   AlphaFoldDB; Q9BU40; -.
DR   SMR; Q9BU40; -.
DR   BioGRID; 124885; 9.
DR   IntAct; Q9BU40; 9.
DR   MINT; Q9BU40; -.
DR   STRING; 9606.ENSP00000361112; -.
DR   GlyCosmos; Q9BU40; 2 sites, No reported glycans.
DR   GlyGen; Q9BU40; 2 sites.
DR   iPTMnet; Q9BU40; -.
DR   PhosphoSitePlus; Q9BU40; -.
DR   BioMuta; CHRDL1; -.
DR   DMDM; 27805644; -.
DR   MassIVE; Q9BU40; -.
DR   PaxDb; 9606-ENSP00000361112; -.
DR   PeptideAtlas; Q9BU40; -.
DR   ProteomicsDB; 12767; -.
DR   ProteomicsDB; 20381; -.
DR   ProteomicsDB; 79052; -. [Q9BU40-3]
DR   Antibodypedia; 365; 307 antibodies from 28 providers.
DR   DNASU; 91851; -.
DR   Ensembl; ENST00000372042.6; ENSP00000361112.1; ENSG00000101938.15. [Q9BU40-4]
DR   Ensembl; ENST00000394797.8; ENSP00000378276.4; ENSG00000101938.15. [Q9BU40-6]
DR   Ensembl; ENST00000444321.2; ENSP00000399739.2; ENSG00000101938.15. [Q9BU40-5]
DR   Ensembl; ENST00000482160.5; ENSP00000418443.1; ENSG00000101938.15. [Q9BU40-3]
DR   GeneID; 91851; -.
DR   KEGG; hsa:91851; -.
DR   MANE-Select; ENST00000372042.6; ENSP00000361112.1; NM_001143981.2; NP_001137453.1. [Q9BU40-4]
DR   UCSC; uc004eou.5; human. [Q9BU40-6]
DR   AGR; HGNC:29861; -.
DR   CTD; 91851; -.
DR   DisGeNET; 91851; -.
DR   GeneCards; CHRDL1; -.
DR   HGNC; HGNC:29861; CHRDL1.
DR   HPA; ENSG00000101938; Tissue enhanced (seminal).
DR   MalaCards; CHRDL1; -.
DR   MIM; 300350; gene.
DR   MIM; 309300; phenotype.
DR   neXtProt; NX_Q9BU40; -.
DR   OpenTargets; ENSG00000101938; -.
DR   Orphanet; 91489; Isolated congenital megalocornea.
DR   PharmGKB; PA134933380; -.
DR   VEuPathDB; HostDB:ENSG00000101938; -.
DR   eggNOG; ENOG502QQFQ; Eukaryota.
DR   GeneTree; ENSGT00940000160983; -.
DR   HOGENOM; CLU_048288_0_0_1; -.
DR   InParanoid; Q9BU40; -.
DR   OMA; EDFRFIF; -.
DR   OrthoDB; 3670395at2759; -.
DR   PhylomeDB; Q9BU40; -.
DR   TreeFam; TF106451; -.
DR   PathwayCommons; Q9BU40; -.
DR   Reactome; R-HSA-201451; Signaling by BMP.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; Q9BU40; -.
DR   BioGRID-ORCS; 91851; 10 hits in 760 CRISPR screens.
DR   ChiTaRS; CHRDL1; human.
DR   GenomeRNAi; 91851; -.
DR   Pharos; Q9BU40; Tbio.
DR   PRO; PR:Q9BU40; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9BU40; Protein.
DR   Bgee; ENSG00000101938; Expressed in decidua and 181 other cell types or tissues.
DR   ExpressionAtlas; Q9BU40; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0036122; F:BMP binding; IBA:GO_Central.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR   GO; GO:0097113; P:AMPA glutamate receptor clustering; IEA:Ensembl.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0000578; P:embryonic axis specification; IEA:Ensembl.
DR   GO; GO:0098976; P:excitatory chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   InterPro; IPR045717; CHRDL1/2.
DR   InterPro; IPR045716; CHRDL_1/2_C.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR46303:SF2; CHORDIN-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR46303; VWFC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF19548; CHRDL_1_2_C; 1.
DR   Pfam; PF00093; VWC; 3.
DR   SMART; SM00214; VWC; 3.
DR   SUPFAM; SSF57603; FnI-like domain; 3.
DR   PROSITE; PS01208; VWFC_1; 3.
DR   PROSITE; PS50184; VWFC_2; 3.
DR   Genevisible; Q9BU40; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Disease variant; Glycoprotein; Neurogenesis; Osteogenesis;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..456
FT                   /note="Chordin-like protein 1"
FT                   /id="PRO_0000005368"
FT   DOMAIN          35..100
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          113..179
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          258..323
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REGION          202..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           179..181
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         100
FT                   /note="P -> PE (in isoform 3)"
FT                   /id="VSP_060078"
FT   VAR_SEQ         101..179
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060079"
FT   VAR_SEQ         328
FT                   /note="K -> KE (in isoform 2, isoform 3 and isoform 4)"
FT                   /id="VSP_060080"
FT   VARIANT         260
FT                   /note="C -> F (in MGC1; dbSNP:rs387906713)"
FT                   /evidence="ECO:0000269|PubMed:22284829"
FT                   /id="VAR_068175"
SQ   SEQUENCE   456 AA;  52026 MW;  345A3C739493A545 CRC64;
     MRKKWKMGGM KYIFSLLFFL LLEGGKTEQV KHSETYCMFQ DKKYRVGERW HPYLEPYGLV
     YCVNCICSEN GNVLCSRVRC PNVHCLSPVH IPHLCCPRCP DSLPPVNNKV TSKSCEYNGT
     TYQHGELFVA EGLFQNRQPN QCTQCSCSEG NVYCGLKTCP KLTCAFPVSV PDSCCRVCRG
     DGELSWEHSD GDIFRQPANR EARHSYHRSH YDPPPSRQAG GLSRFPGARS HRGALMDSQQ
     ASGTIVQIVI NNKHKHGQVC VSNGKTYSHG ESWHPNLRAF GIVECVLCTC NVTKQECKKI
     HCPNRYPCKY PQKIDGKCCK VCPGKKAKEL PGQSFDNKGY FCGEETMPVY ESVFMEDGET
     TRKIALETER PPQVEVHVWT IRKGILQHFH IEKISKRMFE ELPHFKLVTR TTLSQWKIFT
     EGEAQISQMC SSRVCRTELE DLVKVLYLER SEKGHC
//