NCHL1_HUMAN
ID NCHL1_HUMAN Reviewed; 1208 AA.
AC O00533; B7ZL03; Q2M3G2; Q59FY0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Neural cell adhesion molecule L1-like protein;
DE AltName: Full=Close homolog of L1;
DE Contains:
DE RecName: Full=Processed neural cell adhesion molecule L1-like protein;
DE Flags: Precursor;
GN Name=CHL1; Synonyms=CALL;
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 2), TISSUE SPECIFICITY, AND VARIANTS
RP ALA-287 AND VAL-1034.
RX PubMed=9799093; DOI=10.1007/s004390050829;
RA Wei M.-H., Karavanova I., Ivanov S.V., Popescu N.C., Keck C.L., Pack S.,
RA Eisen J.A., Lerman M.I.;
RT "In silico-initiated cloning and molecular characterization of a novel
RT human member of the L1 gene family of neural cell adhesion molecules.";
RL Hum. Genet. 103:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-287
RP AND VAL-1034.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-287
RP AND VAL-1034.
RC TISSUE=Brain;
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-476; ASN-482; ASN-562; ASN-767;
RP ASN-822 AND ASN-1026.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-411.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Extracellular matrix and cell adhesion protein that plays a
CC role in nervous system development and in synaptic plasticity. Both
CC soluble and membranous forms promote neurite outgrowth of cerebellar
CC and hippocampal neurons and suppress neuronal cell death. Plays a role
CC in neuronal positioning of pyramidal neurons and in regulation of both
CC the number of interneurons and the efficacy of GABAergic synapses. May
CC play a role in regulating cell migration in nerve regeneration and
CC cortical development. Potentiates integrin-dependent cell migration
CC towards extracellular matrix proteins. Recruits ANK3 to the plasma
CC membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with L1CAM. May interact with ITGB1/ITGA1
CC heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=Soluble forms produced by
CC cleavage/shedding also exist. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like
CC protein]: Secreted, extracellular space, extracellular matrix
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00533-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00533-2; Sequence=VSP_020082;
CC -!- TISSUE SPECIFICITY: Expressed in the fetal and adult brain as well as
CC in Schwann cell culture. Also detected in adult peripheral tissues.
CC {ECO:0000269|PubMed:9799093}.
CC -!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment region.
CC -!- DOMAIN: The DGEA motif seems to be a recognition site for integrin.
CC -!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
CC generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
CC inhibited by metalloprotease inhibitors (By similarity). Cleaved by
CC BACE1 (By similarity). {ECO:0000250|UniProtKB:P70232}.
CC -!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulfated
CC carbohydrate structure type HNK-1 (SO4-3-GlcUABeta1,3GalBeta1,4GlcNAc)
CC (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92566.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF002246; AAB60937.1; -; mRNA.
DR EMBL; AB209329; BAD92566.1; ALT_INIT; mRNA.
DR EMBL; AC011609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104918; AAI04919.1; -; mRNA.
DR EMBL; BC143496; AAI43497.1; -; mRNA.
DR CCDS; CCDS2556.1; -. [O00533-2]
DR CCDS; CCDS58812.1; -. [O00533-1]
DR RefSeq; NP_001240316.1; NM_001253387.1. [O00533-1]
DR RefSeq; NP_006605.2; NM_006614.3. [O00533-2]
DR RefSeq; XP_006713001.1; XM_006712938.1. [O00533-2]
DR RefSeq; XP_006713002.1; XM_006712939.3. [O00533-2]
DR RefSeq; XP_006713003.1; XM_006712940.3. [O00533-2]
DR RefSeq; XP_011531594.1; XM_011533292.1. [O00533-2]
DR RefSeq; XP_011531596.1; XM_011533294.1. [O00533-1]
DR RefSeq; XP_011531597.1; XM_011533295.1. [O00533-1]
DR RefSeq; XP_016861055.1; XM_017005566.1. [O00533-2]
DR RefSeq; XP_016861056.1; XM_017005567.1. [O00533-2]
DR RefSeq; XP_016861057.1; XM_017005568.1. [O00533-2]
DR RefSeq; XP_016861058.1; XM_017005569.1. [O00533-1]
DR RefSeq; XP_016861059.1; XM_017005570.1. [O00533-1]
DR RefSeq; XP_016861060.1; XM_017005571.1. [O00533-1]
DR AlphaFoldDB; O00533; -.
DR SMR; O00533; -.
DR BioGRID; 115975; 13.
DR IntAct; O00533; 8.
DR STRING; 9606.ENSP00000256509; -.
DR GlyConnect; 1960; 11 N-Linked glycans (9 sites).
DR GlyGen; O00533; 15 sites, 12 N-linked glycans (9 sites).
DR iPTMnet; O00533; -.
DR PhosphoSitePlus; O00533; -.
DR SwissPalm; O00533; -.
DR BioMuta; CHL1; -.
DR EPD; O00533; -.
DR jPOST; O00533; -.
DR MassIVE; O00533; -.
DR MaxQB; O00533; -.
DR PaxDb; O00533; -.
DR PeptideAtlas; O00533; -.
DR PRIDE; O00533; -.
DR ProteomicsDB; 47957; -. [O00533-1]
DR ProteomicsDB; 47958; -. [O00533-2]
DR Antibodypedia; 1160; 134 antibodies from 25 providers.
DR DNASU; 10752; -.
DR Ensembl; ENST00000256509.7; ENSP00000256509.2; ENSG00000134121.10. [O00533-2]
DR Ensembl; ENST00000397491.6; ENSP00000380628.2; ENSG00000134121.10. [O00533-1]
DR GeneID; 10752; -.
DR KEGG; hsa:10752; -.
DR MANE-Select; ENST00000256509.7; ENSP00000256509.2; NM_006614.4; NP_006605.2. [O00533-2]
DR UCSC; uc003bot.4; human. [O00533-1]
DR CTD; 10752; -.
DR DisGeNET; 10752; -.
DR GeneCards; CHL1; -.
DR HGNC; HGNC:1939; CHL1.
DR HPA; ENSG00000134121; Tissue enhanced (brain).
DR MIM; 607416; gene.
DR neXtProt; NX_O00533; -.
DR OpenTargets; ENSG00000134121; -.
DR PharmGKB; PA26470; -.
DR VEuPathDB; HostDB:ENSG00000134121; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160080; -.
DR InParanoid; O00533; -.
DR OMA; HETPPAX; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; O00533; -.
DR TreeFam; TF351098; -.
DR PathwayCommons; O00533; -.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR SignaLink; O00533; -.
DR SIGNOR; O00533; -.
DR BioGRID-ORCS; 10752; 5 hits in 1061 CRISPR screens.
DR ChiTaRS; CHL1; human.
DR GeneWiki; CHL1; -.
DR GenomeRNAi; 10752; -.
DR Pharos; O00533; Tbio.
DR PRO; PR:O00533; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O00533; protein.
DR Bgee; ENSG00000134121; Expressed in cortical plate and 179 other tissues.
DR ExpressionAtlas; O00533; baseline and differential.
DR Genevisible; O00533; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1208
FT /note="Neural cell adhesion molecule L1-like protein"
FT /id="PRO_0000247896"
FT CHAIN 25..?
FT /note="Processed neural cell adhesion molecule L1-like
FT protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000314777"
FT TOPO_DOM 25..1082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 235..328
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..417
FT /note="Ig-like C2-type 4"
FT DOMAIN 423..510
FT /note="Ig-like C2-type 5"
FT DOMAIN 515..607
FT /note="Ig-like C2-type 6"
FT DOMAIN 614..709
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 714..807
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 809..914
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 918..1015
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 693..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 555..558
FT /note="DGEA"
FT MOTIF 1181..1185
FT /note="FIG[AQ]Y"
FT COMPBIAS 1131..1148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 753..754
FT /note="Cleavage; by ADAM8"
FT /evidence="ECO:0000250"
FT SITE 1039..1040
FT /note="Cleavage; by ADAM8"
FT /evidence="ECO:0000250"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70232"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70232"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70232"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 57..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 445..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 536..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 227
FT /note="S -> LKHANDSSSSTEIGSKA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9799093"
FT /id="VSP_020082"
FT VARIANT 17
FT /note="L -> F (in dbSNP:rs2272522)"
FT /id="VAR_027167"
FT VARIANT 287
FT /note="T -> A (in dbSNP:rs13060847)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9799093, ECO:0000269|Ref.2"
FT /id="VAR_027168"
FT VARIANT 411
FT /note="L -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035505"
FT VARIANT 1034
FT /note="I -> V (in dbSNP:rs6442827)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9799093, ECO:0000269|Ref.2"
FT /id="VAR_027169"
FT CARBOHYD O00533-2:231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1208 AA; 135071 MW; F706F87B60A1685D CRC64;
MEPLLLGRGL IVYLMFLLLK FSKAIEIPSS VQQVPTIIKQ SKVQVAFPFD EYFQIECEAK
GNPEPTFSWT KDGNPFYFTD HRIIPSNNSG TFRIPNEGHI SHFQGKYRCF ASNKLGIAMS
EEIEFIVPSV PKFPKEKIDP LEVEEGDPIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
YMSQKGDLYF ANVEEKDSRN DYCCFAAFPR LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP
PTESGSESSI TILKGEILLL ECFAEGLPTP QVDWNKIGGD LPKGRETKEN YGKTLKIENV
SYQDKGNYRC TASNFLGTAT HDFHVIVEEP PRWTKKPQSA VYSTGSNGIL LCEAEGEPQP
TIKWRVNGSP VDNHPFAGDV VFPREISFTN LQPNHTAVYQ CEASNVHGTI LANANIDVVD
VRPLIQTKDG ENYATVVGYS AFLHCEFFAS PEAVVSWQKV EEVKPLEGRR YHIYENGTLQ
INRTTEEDAG SYSCWVENAI GKTAVTANLD IRNATKLRVS PKNPRIPKLH MLELHCESKC
DSHLKHSLKL SWSKDGEAFE INGTEDGRII IDGANLTISN VTLEDQGIYC CSAHTALDSA
ADITQVTVLD VPDPPENLHL SERQNRSVRL TWEAGADHNS NISEYIVEFE GNKEEPGRWE
ELTRVQGKKT TVILPLAPFV RYQFRVIAVN EVGRSQPSQP SDHHETPPAA PDRNPQNIRV
QASQPKEMII KWEPLKSMEQ NGPGLEYRVT WKPQGAPVEW EEETVTNHTL RVMTPAVYAP
YDVKVQAINQ LGSGPDPQSV TLYSGEDYPD TAPVIHGVDV INSTLVKVTW STVPKDRVHG
RLKGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDAFSEFHL TVLAYNSKGA
GPESEPYIFQ TPEGVPEQPT FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY
EIGELNDINI TTPSKPSWHL SNLNATTKYK FYLRACTSQG CGKPITEESS TLGEGSKGIG
KISGVNLTQK THPIEVFEPG AEHIVRLMTK NWGDNDSIFQ DVIETRGREY AGLYDDISTQ
GWFIGLMCAI ALLTLLLLTV CFVKRNRGGK YSVKEKEDLH PDPEIQSVKD ETFGEYSDSD
EKPLKGSLRS LNRDMQPTES ADSLVEYGEG DHGLFSEDGS FIGAYAGSKE KGSVESNGSS
TATFPLRA
