CRDL1_HUMAN
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 03-AUG-2022, entry version 157.
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 GlyGen; Q9BU40; 2 sites.
DR iPTMnet; Q9BU40; -.
DR PhosphoSitePlus; Q9BU40; -.
DR BioMuta; CHRDL1; -.
DR DMDM; 27805644; -.
DR MassIVE; Q9BU40; -.
DR PaxDb; Q9BU40; -.
DR PeptideAtlas; Q9BU40; -.
DR PRIDE; Q9BU40; -.
DR ProteomicsDB; 12767; -.
DR ProteomicsDB; 20381; -.
DR ProteomicsDB; 79052; -. [Q9BU40-3]
DR Antibodypedia; 365; 258 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 CTD; 91851; -.
DR DisGeNET; 91851; -.
DR GeneCards; CHRDL1; -.
DR HGNC; HGNC:29861; CHRDL1.
DR HPA; ENSG00000101938; Tissue enhanced (adipose tissue, seminal vesicle).
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; DYFCGEE; -.
DR OrthoDB; 454087at2759; -.
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; 8 hits in 686 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 179 other tissues.
DR ExpressionAtlas; Q9BU40; baseline and differential.
DR Genevisible; Q9BU40; HS.
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 InterPro; IPR045717; CHRDL1/2.
DR InterPro; IPR045716; CHRDL_1/2_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46303; PTHR46303; 1.
DR Pfam; PF19548; CHRDL_1_2_C; 1.
DR Pfam; PF00093; VWC; 3.
DR SMART; SM00214; VWC; 3.
DR PROSITE; PS01208; VWFC_1; 3.
DR PROSITE; PS50184; VWFC_2; 3.
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
