ICAM5_HUMAN
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 03-AUG-2022, entry version 181.
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 antigen-
RT 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 GlyGen; Q9UMF0; 14 sites.
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; Q9UMF0; -.
DR PeptideAtlas; Q9UMF0; -.
DR PRIDE; Q9UMF0; -.
DR ProteomicsDB; 85189; -.
DR Antibodypedia; 2298; 288 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 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; 731140at2759; -.
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; 18 hits in 1077 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 tissues.
DR ExpressionAtlas; Q9UMF0; baseline and differential.
DR Genevisible; Q9UMF0; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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 Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR013768; ICAM_N.
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 Pfam; PF03921; ICAM_N; 1.
DR Pfam; PF13895; Ig_2; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 8.
DR PROSITE; PS50835; IG_LIKE; 4.
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
