DSCL1_HUMAN
ID DSCL1_HUMAN Reviewed; 2053 AA.
AC Q8TD84; G3V1B5; Q76MU9; Q8IZY3; Q8IZY4; Q8WXU7; Q9ULT7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cell adhesion molecule DSCAML1 {ECO:0000305};
DE AltName: Full=Down syndrome cell adhesion molecule 2;
DE AltName: Full=Down syndrome cell adhesion molecule-like protein 1;
DE Flags: Precursor;
GN Name=DSCAML1; Synonyms=DSCAM2, KIAA1132 {ECO:0000303|PubMed:10574461};
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 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11453658; DOI=10.1006/bbrc.2001.5214;
RA Agarwala K.L., Ganesh S., Tsutsumi Y., Suzuki T., Amano K., Yamakawa K.;
RT "Cloning and functional characterization of DSCAML1, a novel DSCAM-like
RT cell adhesion molecule that mediates homophilic intercellular adhesion.";
RL Biochem. Biophys. Res. Commun. 285:760-772(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=12051741; DOI=10.1016/s0006-291x(02)00307-8;
RA Barlow G.M., Micales B., Chen X.-N., Lyons G.E., Korenberg J.R.;
RT "Mammalian DSCAMs: roles in the development of the spinal cord, cortex, and
RT cerebellum?";
RL Biochem. Biophys. Res. Commun. 293:881-891(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RA Lin S., Wang Z., Ying K., Xie Y., Mao Y.;
RT "DSCAML1, a novel member of the immunoglobulin superfamily.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP STRUCTURE BY NMR OF 979-1087.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second FNIII domain of DSCAML1 protein.";
RL Submitted (FEB-2005) to the PDB data bank.
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-659 AND ILE-1702.
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: Cell adhesion molecule that plays a role in neuronal self-
CC avoidance (PubMed:11453658). Promotes repulsion between specific
CC neuronal processes of either the same cell or the same subtype of
CC cells. Promotes both isoneuronal self-avoidance for creating an orderly
CC neurite arborization in retinal rod bipolar cells and heteroneuronal
CC self-avoidance to maintain mosaic spacing between AII amacrine cells
CC (By similarity). Adhesion molecule that promotes lamina-specific
CC synaptic connections in the retina: expressed in specific subsets of
CC interneurons and retinal ganglion cells (RGCs) and promotes synaptic
CC connectivity via homophilic interactions (By similarity).
CC {ECO:0000250|UniProtKB:E1C8P7, ECO:0000250|UniProtKB:Q4VA61,
CC ECO:0000269|PubMed:11453658}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion. {ECO:0000250|UniProtKB:E1C8P7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11453658};
CC Single-pass type I membrane protein {ECO:0000305}. Synapse
CC {ECO:0000250|UniProtKB:E1C8P7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=1a;
CC IsoId=Q8TD84-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=Q8TD84-2; Sequence=VSP_014978;
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, pancreas, skeletal
CC muscle, kidney and in brain, in particular in the amygdala, caudate
CC nucleus, corpus callosum, hippocampus, substantia nigra, thalamus and
CC subthalamus. {ECO:0000269|PubMed:11453658,
CC ECO:0000269|PubMed:12051741}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM09558.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN32614.1; Type=Miscellaneous discrepancy; Note=Aberrant splice donor site.; Evidence={ECO:0000305};
CC Sequence=BAA86446.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF334384; AAL57166.1; -; mRNA.
DR EMBL; AF491813; AAM09558.1; ALT_INIT; mRNA.
DR EMBL; AF304304; AAN32613.1; -; mRNA.
DR EMBL; AF304305; AAN32614.1; ALT_SEQ; mRNA.
DR EMBL; AB032958; BAA86446.2; ALT_INIT; mRNA.
DR EMBL; AP000711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF511128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67322.1; -; Genomic_DNA.
DR CCDS; CCDS8384.1; -. [Q8TD84-1]
DR RefSeq; NP_065744.2; NM_020693.3. [Q8TD84-1]
DR PDB; 1VA9; NMR; -; A=979-1087.
DR PDBsum; 1VA9; -.
DR AlphaFoldDB; Q8TD84; -.
DR SMR; Q8TD84; -.
DR BioGRID; 121525; 5.
DR IntAct; Q8TD84; 3.
DR STRING; 9606.ENSP00000315465; -.
DR GlyGen; Q8TD84; 21 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TD84; -.
DR PhosphoSitePlus; Q8TD84; -.
DR BioMuta; DSCAML1; -.
DR DMDM; 73620825; -.
DR MassIVE; Q8TD84; -.
DR PaxDb; Q8TD84; -.
DR PeptideAtlas; Q8TD84; -.
DR PRIDE; Q8TD84; -.
DR ProteomicsDB; 32317; -.
DR ProteomicsDB; 74248; -. [Q8TD84-1]
DR ProteomicsDB; 74249; -. [Q8TD84-2]
DR Antibodypedia; 62371; 26 antibodies from 15 providers.
DR DNASU; 57453; -.
DR Ensembl; ENST00000527706.5; ENSP00000434335.1; ENSG00000177103.15. [Q8TD84-2]
DR Ensembl; ENST00000651296.2; ENSP00000498769.1; ENSG00000177103.15. [Q8TD84-1]
DR GeneID; 57453; -.
DR KEGG; hsa:57453; -.
DR MANE-Select; ENST00000651296.2; ENSP00000498769.1; NM_020693.4; NP_065744.3.
DR UCSC; uc001prh.1; human. [Q8TD84-1]
DR UCSC; uc058hud.1; human.
DR CTD; 57453; -.
DR DisGeNET; 57453; -.
DR GeneCards; DSCAML1; -.
DR HGNC; HGNC:14656; DSCAML1.
DR HPA; ENSG00000177103; Group enriched (brain, retina).
DR MIM; 611782; gene.
DR neXtProt; NX_Q8TD84; -.
DR OpenTargets; ENSG00000177103; -.
DR PharmGKB; PA38384; -.
DR VEuPathDB; HostDB:ENSG00000177103; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155354; -.
DR HOGENOM; CLU_001038_0_1_1; -.
DR InParanoid; Q8TD84; -.
DR OrthoDB; 14047at2759; -.
DR PhylomeDB; Q8TD84; -.
DR TreeFam; TF316846; -.
DR PathwayCommons; Q8TD84; -.
DR Reactome; R-HSA-376172; DSCAM interactions.
DR SignaLink; Q8TD84; -.
DR SIGNOR; Q8TD84; -.
DR BioGRID-ORCS; 57453; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; DSCAML1; human.
DR EvolutionaryTrace; Q8TD84; -.
DR GenomeRNAi; 57453; -.
DR Pharos; Q8TD84; Tbio.
DR PRO; PR:Q8TD84; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8TD84; protein.
DR Bgee; ENSG00000177103; Expressed in cortical plate and 130 other tissues.
DR ExpressionAtlas; Q8TD84; baseline and differential.
DR Genevisible; Q8TD84; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; NAS:UniProtKB.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 16.
DR InterPro; IPR033029; DSCAML1.
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; IPR013106; Ig_V-set.
DR PANTHER; PTHR13817:SF54; PTHR13817:SF54; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 10.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 10.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 10.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Neurogenesis; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2053
FT /note="Cell adhesion molecule DSCAML1"
FT /id="PRO_0000014748"
FT TOPO_DOM 19..1591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1613..2053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..119
FT /note="Ig-like C2-type 1"
FT DOMAIN 115..217
FT /note="Ig-like C2-type 2"
FT DOMAIN 226..306
FT /note="Ig-like C2-type 3"
FT DOMAIN 314..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..501
FT /note="Ig-like C2-type 5"
FT DOMAIN 506..586
FT /note="Ig-like C2-type 6"
FT DOMAIN 596..685
FT /note="Ig-like C2-type 7"
FT DOMAIN 690..784
FT /note="Ig-like C2-type 8"
FT DOMAIN 788..885
FT /note="Ig-like C2-type 9"
FT DOMAIN 887..984
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 989..1088
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1093..1189
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1193..1288
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1278..1377
FT /note="Ig-like C2-type 10"
FT DOMAIN 1383..1477
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1478..1578
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1715..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1974..2053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2025..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 247..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 336..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 429..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 526..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 617..669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 711..767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 810..867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1311..1363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 35..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_014978"
FT VARIANT 659
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs533175875)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035512"
FT VARIANT 1702
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs147907435)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035513"
FT CONFLICT 4
FT /note="V -> L (in Ref. 3; AAN32613/AAN32614)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..152
FT /note="SSV -> FLG (in Ref. 3; AAN32613)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="H -> N (in Ref. 1; AAL57166 and 4; BAA86446)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="S -> P (in Ref. 3; AAN32614)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="H -> Y (in Ref. 3; AAN32613)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="Y -> D (in Ref. 3; AAN32613/AAN32614)"
FT /evidence="ECO:0000305"
FT STRAND 991..997
FT /evidence="ECO:0007829|PDB:1VA9"
FT STRAND 999..1008
FT /evidence="ECO:0007829|PDB:1VA9"
FT STRAND 1021..1030
FT /evidence="ECO:0007829|PDB:1VA9"
FT STRAND 1046..1055
FT /evidence="ECO:0007829|PDB:1VA9"
FT STRAND 1062..1070
FT /evidence="ECO:0007829|PDB:1VA9"
SQ SEQUENCE 2053 AA; 224463 MW; 9CC9644214FF19C4 CRC64;
MWLVTFLLLL DSLHKARPED VGTSLYFVND SLQQVTFSSS VGVVVPCPAA GSPSAALRWY
LATGDDIYDV PHIRHVHANG TLQLYPFSPS AFNSFIHDND YFCTAENAAG KIRSPNIRVK
AVFREPYTVR VEDQRSMRGN VAVFKCLIPS SVQEYVSVVS WEKDTVSIIP EHRFFITYHG
GLYISDVQKE DALSTYRCIT KHKYSGETRQ SNGARLSVTD PAESIPTILD GFHSQEVWAG
HTVELPCTAS GYPIPAIRWL KDGRPLPADS RWTKRITGLT ISDLRTEDSG TYICEVTNTF
GSAEATGILM VIDPLHVTLT PKKLKTGIGS TVILSCALTG SPEFTIRWYR NTELVLPDEA
ISIRGLSNET LLITSAQKSH SGAYQCFATR KAQTAQDFAI IALEDGTPRI VSSFSEKVVN
PGEQFSLMCA AKGAPPPTVT WALDDEPIVR DGSHRTNQYT MSDGTTISHM NVTGPQIRDG
GVYRCTARNL VGSAEYQARI NVRGPPSIRA MRNITAVAGR DTLINCRVIG YPYYSIKWYK
DALLLPDNHR QVVFENGTLK LTDVQKGMDE GEYLCSVLIQ PQLSISQSVH VAVKVPPLIQ
PFEFPPASIG QLLYIPCVVS SGDMPIRITW RKDGQVIISG SGVTIESKEF MSSLQISSVS
LKHNGNYTCI ASNAAATVSR ERQLIVRVPP RFVVQPNNQD GIYGKAGVLN CSVDGYPPPK
VMWKHAKGSG NPQQYHPVPL TGRIQILPNS SLLIRHVLEE DIGYYLCQAS NGVGTDISKS
MFLTVKIPAM ITSHPNTTIA IKGHAKELNC TARGERPIII RWEKGDTVID PDRVMRYAIA
TKDNGDEVVS TLKLKPADRG DSVFFSCHAI NSYGEDRGLI QLTVQEPPDP PELEIREVKA
RSMNLRWTQR FDGNSIITGF DIEYKNKSDS WDFKQSTRNI SPTINQANIV DLHPASVYSI
RMYSFNKIGR SEPSKELTIS TEEAAPDGPP MDVTLQPVTS QSIQVTWKAP KKELQNGVIR
GYQIGYRENS PGSNGQYSIV EMKATGDSEV YTLDNLKKFA QYGVVVQAFN RAGTGPSSSE
INATTLEDVP SQPPENVRAL SITSDVAVIS WSEPPRSTLN GVLKGYRVIF WSLYVDGEWG
EMQNITTTRE RVELRGMEKF TNYSVQVLAY TQAGDGVRSS VLYIQTKEDV PGPPAGIKAV
PSSASSVVVS WLPPTKPNGV IRKYTIFCSS PGSGQPAPSE YETSPEQLFY RIAHLNRGQQ
YLLWVAAVTS AGRGNSSEKV TIEPAGKAPA KIISFGGTVT TPWMKDVRLP CNSVGDPAPA
VKWTKDSEDS AIPVSMDGHR LIHTNGTLLL RAVKAEDSGY YTCTATNTGG FDTIIVNLLV
QVPPDQPRLT VSKTSASSIT LTWIPGDNGG SSIRGFVLQY SVDNSEEWKD VFISSSERSF
KLDSLKCGTW YKVKLAAKNS VGSGRISEII EAKTHGREPS FSKDQHLFTH INSTHARLNL
QGWNNGGCPI TAIVLEYRPK GTWAWQGLRA NSSGEVFLTE LREATWYELR MRACNSAGCG
NETAQFATLD YDGSTIPPIK SAQGEGDDVK KLFTIGCPVI LATLGVALLF IVRKKRKEKR
LKRLRDAKSL AEMLISKNNR SFDTPVKGPP QGPRLHIDIP RVQLLIEDKE GIKQLGDDKA
TIPVTDAEFS QAVNPQSFCT GVSLHHPTLI QSTGPLIDMS DIRPGTNPVS RKNVKSAHST
RNRYSSQWTL TKCQASTPAR TLTSDWRTVG SQHGVTVTES DSYSASLSQD TDKGRNSMVS
TESASSTYEE LARAYEHAKL EEQLQHAKFE ITECFISDSS SDQMTTGTNE NADSMTSMST
PSEPGICRFT ASPPKPQDAD RGKNVAVPIP HRANKSDYCN LPLYAKSEAF FRKADGREPC
PVVPPREASI RNLARTYHTQ ARHLTLDPAS KSLGLPHPGA PAAASTATLP QRTLAMPAPP
AGTAPPAPGP TPAEPPTAPS AAPPAPSTEP PRAGGPHTKM GGSRDSLLEM STSGVGRSQK
QGAGAYSKSY TLV
