ID   ICAM5_HUMAN             Reviewed;         924 AA.
AC   Q9UMF0; Q9Y6F3;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Intercellular adhesion molecule 5;
DE            Short=ICAM-5;
DE   AltName: Full=Telencephalin;
DE   Flags: Precursor;
GN   Name=ICAM5; Synonyms=TLCN, TLN;
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], AND VARIANTS ILE-301 AND THR-348.
RC   TISSUE=Brain;
RX   PubMed=8995416; DOI=10.1074/jbc.272.2.1156;
RA   Mizuno T., Yoshihara Y., Inazawa J., Kagamiyama H., Mori K.;
RT   "cDNA cloning and chromosomal localization of the human telencephalin and
RT   its distinctive interaction with lymphocyte function-associated
RT   antigen-1.";
RL   J. Biol. Chem. 272:1156-1163(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9828136; DOI=10.1006/geno.1998.5565;
RA   Kilgannon P., Turner T., Meyer J., Wisdom W., Gallatin W.M.;
RT   "Mapping of the ICAM-5 (telencephalin) gene, a neuronal member of the ICAM
RT   family, to a location between ICAM-1 and ICAM-3 on human chromosome
RT   19p13.2.";
RL   Genomics 54:328-330(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND THR-184, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=15144186; DOI=10.1021/ac035352d;
RA   Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA   Peters E.C.;
RT   "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT   human T cells using immobilized metal affinity chromatography and tandem
RT   mass spectrometry.";
RL   Anal. Chem. 76:2763-2772(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-227 IN COMPLEX WITH ITGAL,
RP   GLYCOSYLATION AT ASN-54; ASN-74; ASN-137; ASN-195 AND ASN-214, AND
RP   DISULFIDE BONDS.
RX   PubMed=18691975; DOI=10.1016/j.molcel.2008.06.022;
RA   Zhang H., Casasnovas J.M., Jin M., Liu J.H., Gahmberg C.G., Springer T.A.,
RA   Wang J.H.;
RT   "An unusual allosteric mobility of the C-terminal helix of a high-affinity
RT   alphaL integrin I domain variant bound to ICAM-5.";
RL   Mol. Cell 31:432-437(2008).
RN   [6]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-140; TRP-188 AND GLN-488.
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: ICAM proteins are ligands for the leukocyte adhesion protein
CC       LFA-1 (integrin alpha-L/beta-2).
CC   -!- INTERACTION:
CC       Q9UMF0; Q99996-3: AKAP9; NbExp=3; IntAct=EBI-6398041, EBI-11022349;
CC       Q9UMF0; P13196: ALAS1; NbExp=3; IntAct=EBI-6398041, EBI-3905054;
CC       Q9UMF0; Q9NP70: AMBN; NbExp=3; IntAct=EBI-6398041, EBI-11893530;
CC       Q9UMF0; P05067: APP; NbExp=3; IntAct=EBI-6398041, EBI-77613;
CC       Q9UMF0; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-6398041, EBI-25843552;
CC       Q9UMF0; Q9HCU0: CD248; NbExp=3; IntAct=EBI-6398041, EBI-9680942;
CC       Q9UMF0; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-6398041, EBI-25836090;
CC       Q9UMF0; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-6398041, EBI-2872414;
CC       Q9UMF0; Q9H410: DSN1; NbExp=3; IntAct=EBI-6398041, EBI-1001144;
CC       Q9UMF0; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-6398041, EBI-3893327;
CC       Q9UMF0; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-6398041, EBI-25835236;
CC       Q9UMF0; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-6398041, EBI-2857315;
CC       Q9UMF0; P51674: GPM6A; NbExp=3; IntAct=EBI-6398041, EBI-7187133;
CC       Q9UMF0; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-6398041, EBI-2868501;
CC       Q9UMF0; Q13887: KLF5; NbExp=3; IntAct=EBI-6398041, EBI-2696013;
CC       Q9UMF0; Q96NJ5: KLHL32; NbExp=3; IntAct=EBI-6398041, EBI-6426390;
CC       Q9UMF0; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-6398041, EBI-8473062;
CC       Q9UMF0; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-6398041, EBI-2350424;
CC       Q9UMF0; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-6398041, EBI-741037;
CC       Q9UMF0; P02795: MT2A; NbExp=3; IntAct=EBI-6398041, EBI-996616;
CC       Q9UMF0; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-6398041, EBI-6952711;
CC       Q9UMF0; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-6398041, EBI-1058491;
CC       Q9UMF0; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-6398041, EBI-11984839;
CC       Q9UMF0; Q96EN9: REX1BD; NbExp=3; IntAct=EBI-6398041, EBI-745810;
CC       Q9UMF0; Q96EP0: RNF31; NbExp=3; IntAct=EBI-6398041, EBI-948111;
CC       Q9UMF0; O75528: TADA3; NbExp=3; IntAct=EBI-6398041, EBI-473249;
CC       Q9UMF0; P45880: VDAC2; NbExp=3; IntAct=EBI-6398041, EBI-354022;
CC       Q9UMF0; P05094: ACTN1; Xeno; NbExp=3; IntAct=EBI-6398041, EBI-5847257;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed on neurons in the most rostral segment of
CC       the mammalian brain, the telencephalon.
CC   -!- PTM: Glycosylation at Asn-54 is critical for functional folding.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC       {ECO:0000305}.
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DR   EMBL; U72671; AAC50959.1; -; mRNA.
DR   EMBL; AF082802; AAC97931.1; -; Genomic_DNA.
DR   EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS12233.1; -.
DR   RefSeq; NP_003250.3; NM_003259.3.
DR   RefSeq; XP_011526531.1; XM_011528229.1.
DR   PDB; 3BN3; X-ray; 2.10 A; B=32-227.
DR   PDB; 4OI9; X-ray; 2.50 A; A=32-409.
DR   PDB; 4OIA; X-ray; 3.70 A; A/B=32-409.
DR   PDB; 4OIB; X-ray; 3.50 A; A=32-409.
DR   PDBsum; 3BN3; -.
DR   PDBsum; 4OI9; -.
DR   PDBsum; 4OIA; -.
DR   PDBsum; 4OIB; -.
DR   AlphaFoldDB; Q9UMF0; -.
DR   SMR; Q9UMF0; -.
DR   BioGRID; 112942; 67.
DR   IntAct; Q9UMF0; 48.
DR   STRING; 9606.ENSP00000221980; -.
DR   GlyCosmos; Q9UMF0; 14 sites, No reported glycans.
DR   GlyGen; Q9UMF0; 15 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UMF0; -.
DR   PhosphoSitePlus; Q9UMF0; -.
DR   BioMuta; ICAM5; -.
DR   DMDM; 296439327; -.
DR   EPD; Q9UMF0; -.
DR   jPOST; Q9UMF0; -.
DR   MassIVE; Q9UMF0; -.
DR   MaxQB; Q9UMF0; -.
DR   PaxDb; 9606-ENSP00000221980; -.
DR   PeptideAtlas; Q9UMF0; -.
DR   ProteomicsDB; 85189; -.
DR   Antibodypedia; 2298; 336 antibodies from 37 providers.
DR   DNASU; 7087; -.
DR   Ensembl; ENST00000221980.5; ENSP00000221980.3; ENSG00000105376.5.
DR   GeneID; 7087; -.
DR   KEGG; hsa:7087; -.
DR   MANE-Select; ENST00000221980.5; ENSP00000221980.3; NM_003259.4; NP_003250.3.
DR   UCSC; uc002mnu.5; human.
DR   AGR; HGNC:5348; -.
DR   CTD; 7087; -.
DR   DisGeNET; 7087; -.
DR   GeneCards; ICAM5; -.
DR   HGNC; HGNC:5348; ICAM5.
DR   HPA; ENSG00000105376; Tissue enriched (brain).
DR   MIM; 601852; gene.
DR   neXtProt; NX_Q9UMF0; -.
DR   OpenTargets; ENSG00000105376; -.
DR   PharmGKB; PA29596; -.
DR   VEuPathDB; HostDB:ENSG00000105376; -.
DR   eggNOG; ENOG502QS16; Eukaryota.
DR   GeneTree; ENSGT00940000162184; -.
DR   HOGENOM; CLU_014560_0_0_1; -.
DR   InParanoid; Q9UMF0; -.
DR   OMA; GCPSNWT; -.
DR   OrthoDB; 4014106at2759; -.
DR   PhylomeDB; Q9UMF0; -.
DR   TreeFam; TF333745; -.
DR   PathwayCommons; Q9UMF0; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   SignaLink; Q9UMF0; -.
DR   BioGRID-ORCS; 7087; 20 hits in 1157 CRISPR screens.
DR   EvolutionaryTrace; Q9UMF0; -.
DR   GeneWiki; ICAM5; -.
DR   GenomeRNAi; 7087; -.
DR   Pharos; Q9UMF0; Tbio.
DR   PRO; PR:Q9UMF0; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9UMF0; Protein.
DR   Bgee; ENSG00000105376; Expressed in right frontal lobe and 97 other cell types or tissues.
DR   ExpressionAtlas; Q9UMF0; baseline and differential.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR   GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR   GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
DR   CDD; cd05755; IgC2_2_ICAM-1_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   InterPro; IPR003988; ICAM.
DR   InterPro; IPR048679; ICAM1_3_5_D2.
DR   InterPro; IPR013768; ICAM_N.
DR   InterPro; IPR047012; ICAM_VCAM.
DR   InterPro; IPR003987; ICAM_VCAM_N.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR   PANTHER; PTHR13771:SF9; INTERCELLULAR ADHESION MOLECULE 5; 1.
DR   Pfam; PF21146; ICAM1_3_5_D2; 1.
DR   Pfam; PF03921; ICAM_N; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   PRINTS; PR01473; ICAM.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF48726; Immunoglobulin; 8.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   Genevisible; Q9UMF0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..924
FT                   /note="Intercellular adhesion molecule 5"
FT                   /id="PRO_0000014799"
FT   TOPO_DOM        32..835
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        836..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        857..924
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          48..130
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          135..235
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          242..329
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          337..402
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          408..486
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          491..568
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          573..662
FT                   /note="Ig-like C2-type 7"
FT   DOMAIN          666..739
FT                   /note="Ig-like C2-type 8"
FT   DOMAIN          746..830
FT                   /note="Ig-like C2-type 9"
FT   REGION          891..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         182
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:15144186"
FT   MOD_RES         184
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:15144186"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000305|PubMed:18691975"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18691975"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18691975"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18691975"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18691975"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        764
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        795
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        796
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..99
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:18691975"
FT   DISULFID        59..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:18691975"
FT   DISULFID        142..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:18691975"
FT   DISULFID        249..302
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        344..383
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        415..470
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        498..552
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        580..645
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        673..725
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        769..814
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VARIANT         140
FT                   /note="L -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035515"
FT   VARIANT         188
FT                   /note="R -> W (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035516"
FT   VARIANT         301
FT                   /note="V -> I (in dbSNP:rs1056538)"
FT                   /evidence="ECO:0000269|PubMed:8995416"
FT                   /id="VAR_056046"
FT   VARIANT         348
FT                   /note="A -> T (in dbSNP:rs2228615)"
FT                   /evidence="ECO:0000269|PubMed:8995416"
FT                   /id="VAR_056047"
FT   VARIANT         488
FT                   /note="E -> Q (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035517"
FT   CONFLICT        614
FT                   /note="A -> T (in Ref. 1; AAC50959)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        786
FT                   /note="G -> R (in Ref. 2; AAC97931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        816
FT                   /note="A -> R (in Ref. 1; AAC50959 and 2; AAC97931)"
FT                   /evidence="ECO:0000305"
FT   STRAND          36..46
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          49..57
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          70..79
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          82..90
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          106..111
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          136..144
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          153..159
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          162..168
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          179..186
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          195..203
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          211..215
FT                   /evidence="ECO:0007829|PDB:3BN3"
FT   STRAND          223..226
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          253..256
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          261..271
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          281..288
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          295..306
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          309..320
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          326..330
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          332..335
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          339..345
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          348..354
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          366..371
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   HELIX           374..376
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          379..389
FT                   /evidence="ECO:0007829|PDB:4OI9"
FT   STRAND          392..405
FT                   /evidence="ECO:0007829|PDB:4OI9"
SQ   SEQUENCE   924 AA;  97116 MW;  97D0A9467BD16D30 CRC64;
     MPGPSPGLRR ALLGLWAALG LGLFGLSAVS QEPFWADLQP RVAFVERGGS LWLNCSTNCP
     RPERGGLETS LRRNGTQRGL RWLARQLVDI REPETQPVCF FRCARRTLQA RGLIRTFQRP
     DRVELMPLPP WQPVGENFTL SCRVPGAGPR ASLTLTLLRG AQELIRRSFA GEPPRARGAV
     LTATVLARRE DHGANFSCRA ELDLRPHGLG LFENSSAPRE LRTFSLSPDA PRLAAPRLLE
     VGSERPVSCT LDGLFPASEA RVYLALGDQN LSPDVTLEGD AFVATATATA SAEQEGARQL
     VCNVTLGGEN RETRENVTIY SFPAPLLTLS EPSVSEGQMV TVTCAAGAQA LVTLEGVPAA
     VPGQPAQLQL NATENDDRRS FFCDATLDVD GETLIKNRSA ELRVLYAPRL DDSDCPRSWT
     WPEGPEQTLR CEARGNPEPS VHCARSDGGA VLALGLLGPV TRALSGTYRC KAANDQGEAV
     KDVTLTVEYA PALDSVGCPE RITWLEGTEA SLSCVAHGVP PPDVICVRSG ELGAVIEGLL
     RVAREHAGTY RCEATNPRGS AAKNVAVTVE YGPRFEEPSC PSNWTWVEGS GRLFSCEVDG
     KPQPSVKCVG SGGATEGVLL PLAPPDPSPR APRIPRVLAP GIYVCNATNR HGSVAKTVVV
     SAESPPEMDE STCPSHQTWL EGAEASALAC AARGRPSPGV RCSREGIPWP EQQRVSREDA
     GTYHCVATNA HGTDSRTVTV GVEYRPVVAE LAASPPGGVR PGGNFTLTCR AEAWPPAQIS
     WRAPPGALNI GLSSNNSTLS VAGAMGSHGG EYECAATNAH GRHARRITVR VAGPWLWVAV
     GGAAGGAALL AAGAGLAFYV QSTACKKGEY NVQEAESSGE AVCLNGAGGG AGGAAGAEGG
     PEAAGGAAES PAEGEVFAIQ LTSA
//