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   27-MAR-2024, entry version 182.
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};
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; 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.
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   GlyCosmos; O00533; 15 sites, 12 glycans.
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; 9606-ENSP00000256509; -.
DR   PeptideAtlas; O00533; -.
DR   ProteomicsDB; 47957; -. [O00533-1]
DR   ProteomicsDB; 47958; -. [O00533-2]
DR   Antibodypedia; 1160; 154 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   AGR; HGNC:1939; -.
DR   CTD; 10752; -.
DR   DisGeNET; 10752; -.
DR   GeneCards; CHL1; -.
DR   HGNC; HGNC:1939; CHL1.
DR   HPA; ENSG00000134121; Tissue enhanced (brain, ovary).
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; RARHEFH; -.
DR   OrthoDB; 2912783at2759; -.
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; 9 hits in 1141 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 181 other cell types or tissues.
DR   ExpressionAtlas; O00533; baseline and differential.
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:0016020; C: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   CDD; cd00096; Ig; 1.
DR   CDD; cd05731; Ig3_L1-CAM_like; 1.
DR   CDD; cd04978; Ig4_L1-NrCAM_like; 1.
DR   CDD; cd05845; IgI_2_L1-CAM_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; PTHR44170:SF51; NEURAL CELL ADHESION MOLECULE L1-LIKE PROTEIN ISOFORM X1; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF13882; Bravo_FIGEY; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   Genevisible; O00533; HS.
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
//