ID AGRG4_HUMAN Reviewed; 3080 AA. AC Q8IZF6; A2A2J1; A2A2J2; Q5EGP2; Q86SM6; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 24-JAN-2024, entry version 163. DE RecName: Full=Adhesion G-protein coupled receptor G4 {ECO:0000303|PubMed:25713288}; DE AltName: Full=G-protein coupled receptor 112; DE Flags: Precursor; GN Name=ADGRG4; Synonyms=GPR112; 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). RX PubMed=12435584; DOI=10.1016/s0014-5793(02)03574-3; RA Fredriksson R., Lagerstroem M.C., Hoeglund P.J., Schioeth H.B.; RT "Novel human G protein-coupled receptors with long N-terminals containing RT GPS domains and Ser/Thr-rich regions."; RL FEBS Lett. 531:407-414(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-276 AND HIS-368. RC TISSUE=Retina; RA Bonner T.I., Kauffman D., Nagle J.W., Sloger M., Kozhich O.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 343-1613 (ISOFORMS 1/2). RX PubMed=12679517; DOI=10.1073/pnas.0230374100; RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E., RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C., RA Bergmann J.E., Gaitanaris G.A.; RT "The G protein-coupled receptor repertoires of human and mouse."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003). RN [5] RP TISSUE SPECIFICITY. RX PubMed=18953328; DOI=10.1038/modpathol.2008.174; RA Leja J., Essaghir A., Essand M., Wester K., Oeberg K., Toetterman T.H., RA Lloyd R., Vasmatzis G., Demoulin J.-B., Giandomenico V.; RT "Novel markers for enterochromaffin cells and gastrointestinal RT neuroendocrine carcinomas."; RL Mod. Pathol. 22:261-272(2009). RN [6] RP NOMENCLATURE. RX PubMed=25713288; DOI=10.1124/pr.114.009647; RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R., RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I., RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S., RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A., RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.; RT "International union of basic and clinical pharmacology. XCIV. Adhesion G RT protein-coupled receptors."; RL Pharmacol. Rev. 67:338-367(2015). CC -!- FUNCTION: Orphan receptor. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane CC protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8IZF6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IZF6-2; Sequence=VSP_038170, VSP_038173, VSP_038174, CC VSP_038175, VSP_038176; CC Name=3; CC IsoId=Q8IZF6-3; Sequence=VSP_038171, VSP_038172; CC -!- TISSUE SPECIFICITY: Detected in fetal retina. Highly expressed in CC normal enterochromaffin cells and in neuroendocrine carcinoma. Detected CC in normal liver; highly expressed in primary liver carcinoma. CC {ECO:0000269|PubMed:18953328}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. CC Adhesion G-protein coupled receptor (ADGR) subfamily. {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; AY140954; AAN46668.1; -; mRNA. DR EMBL; AY882585; AAW78659.1; -; mRNA. DR EMBL; AL078638; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136167; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL161778; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY255581; AAO85093.1; -; mRNA. DR CCDS; CCDS35409.1; -. [Q8IZF6-1] DR RefSeq; NP_722576.3; NM_153834.3. [Q8IZF6-1] DR RefSeq; XP_011529571.1; XM_011531269.2. [Q8IZF6-1] DR PDB; 7WUJ; EM; 3.30 A; E=2720-3080. DR PDB; 8B55; X-ray; 1.36 A; A=26-240. DR PDBsum; 7WUJ; -. DR PDBsum; 8B55; -. DR EMDB; EMD-32837; -. DR SASBDB; Q8IZF6; -. DR SMR; Q8IZF6; -. DR BioGRID; 126563; 5. DR IntAct; Q8IZF6; 2. DR STRING; 9606.ENSP00000377699; -. DR MEROPS; P02.014; -. DR GlyCosmos; Q8IZF6; 8 sites, No reported glycans. DR GlyGen; Q8IZF6; 8 sites. DR iPTMnet; Q8IZF6; -. DR PhosphoSitePlus; Q8IZF6; -. DR BioMuta; ADGRG4; -. DR DMDM; 259016241; -. DR EPD; Q8IZF6; -. DR jPOST; Q8IZF6; -. DR MassIVE; Q8IZF6; -. DR PaxDb; 9606-ENSP00000377699; -. DR PeptideAtlas; Q8IZF6; -. DR ProteomicsDB; 71345; -. [Q8IZF6-1] DR ProteomicsDB; 71346; -. [Q8IZF6-2] DR ProteomicsDB; 71347; -. [Q8IZF6-3] DR Antibodypedia; 51733; 55 antibodies from 17 providers. DR DNASU; 139378; -. DR Ensembl; ENST00000370652.5; ENSP00000359686.1; ENSG00000156920.11. [Q8IZF6-1] DR Ensembl; ENST00000394141.1; ENSP00000377697.1; ENSG00000156920.11. [Q8IZF6-3] DR Ensembl; ENST00000394143.6; ENSP00000377699.1; ENSG00000156920.11. [Q8IZF6-1] DR GeneID; 139378; -. DR KEGG; hsa:139378; -. DR MANE-Select; ENST00000394143.6; ENSP00000377699.1; NM_153834.4; NP_722576.3. DR UCSC; uc004ezu.1; human. [Q8IZF6-1] DR AGR; HGNC:18992; -. DR CTD; 139378; -. DR GeneCards; ADGRG4; -. DR HGNC; HGNC:18992; ADGRG4. DR HPA; ENSG00000156920; Tissue enhanced (fallopian tube, intestine, retina). DR MIM; 301085; gene. DR neXtProt; NX_Q8IZF6; -. DR OpenTargets; ENSG00000156920; -. DR PharmGKB; PA134885132; -. DR VEuPathDB; HostDB:ENSG00000156920; -. DR eggNOG; KOG4193; Eukaryota. DR GeneTree; ENSGT00940000162744; -. DR HOGENOM; CLU_000643_0_0_1; -. DR InParanoid; Q8IZF6; -. DR OMA; MMDQPQN; -. DR OrthoDB; 4893596at2759; -. DR PhylomeDB; Q8IZF6; -. DR TreeFam; TF321769; -. DR PathwayCommons; Q8IZF6; -. DR SignaLink; Q8IZF6; -. DR BioGRID-ORCS; 139378; 22 hits in 776 CRISPR screens. DR ChiTaRS; ADGRG4; human. DR GeneWiki; GPR112; -. DR GenomeRNAi; 139378; -. DR Pharos; Q8IZF6; Tdark. DR PRO; PR:Q8IZF6; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q8IZF6; Protein. DR Bgee; ENSG00000156920; Expressed in duodenum and 40 other cell types or tissues. DR GO; GO:0016020; C:membrane; TAS:GDB. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB. DR CDD; cd15997; 7tmB2_GPR112; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.220.50; -; 1. DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR046338; GAIN_dom_sf. DR InterPro; IPR017981; GPCR_2-like_7TM. DR InterPro; IPR036445; GPCR_2_extracell_dom_sf. DR InterPro; IPR000832; GPCR_2_secretin-like. DR InterPro; IPR017983; GPCR_2_secretin-like_CS. DR InterPro; IPR000203; GPS. DR InterPro; IPR001759; Pentraxin-related. DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR12011:SF277; ADHESION G-PROTEIN COUPLED RECEPTOR G4; 1. DR Pfam; PF00002; 7tm_2; 1. DR Pfam; PF01825; GPS; 1. DR Pfam; PF00354; Pentaxin; 1. DR PRINTS; PR00249; GPCRSECRETIN. DR SMART; SM00303; GPS; 1. DR SMART; SM00159; PTX; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR PROSITE; PS50221; GPS; 1. DR PROSITE; PS51828; PTX_2; 1. DR Genevisible; Q8IZF6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..3080 FT /note="Adhesion G-protein coupled receptor G4" FT /id="PRO_0000070335" FT TOPO_DOM 28..2741 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 2742..2762 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 2763..2778 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 2779..2799 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 2800..2805 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 2806..2826 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 2827..2848 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 2849..2869 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 2870..2892 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 2893..2913 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 2914..2942 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 2943..2963 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 2964..2965 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 2966..2986 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 2987..3080 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 29..228 FT /note="Pentraxin (PTX)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172" FT DOMAIN 2682..2733 FT /note="GPS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098" FT REGION 946..965 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1274..1348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2109..2141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3051..3080 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3051..3065 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 233 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 487 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 836 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 899 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1020 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1519 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2361 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2640 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 58..123 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172" FT VAR_SEQ 1..63 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12435584" FT /id="VSP_038170" FT VAR_SEQ 24 FT /note="D -> V (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_038171" FT VAR_SEQ 25..229 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_038172" FT VAR_SEQ 2243..2381 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12435584" FT /id="VSP_038173" FT VAR_SEQ 2593..2637 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12435584" FT /id="VSP_038174" FT VAR_SEQ 2979..3012 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12435584" FT /id="VSP_038175" FT VAR_SEQ 3069..3080 FT /note="DDFDKDPYCSSP -> APELSALHVVASEPTTG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12435584" FT /id="VSP_038176" FT VARIANT 276 FT /note="I -> M (in dbSNP:rs4829829)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_055929" FT VARIANT 368 FT /note="P -> H (in dbSNP:rs5930931)" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_059329" FT VARIANT 1213 FT /note="T -> N (in dbSNP:rs4829830)" FT /id="VAR_059330" FT VARIANT 1540 FT /note="S -> P (in dbSNP:rs912002)" FT /id="VAR_059331" FT VARIANT 1791 FT /note="F -> L (in dbSNP:rs5930932)" FT /id="VAR_059332" FT CONFLICT 229 FT /note="Missing (in Ref. 1; AAN46668)" FT /evidence="ECO:0000305" FT CONFLICT 2426 FT /note="Missing (in Ref. 1; AAN46668)" FT /evidence="ECO:0000305" FT CONFLICT 2694 FT /note="Missing (in Ref. 1; AAN46668)" FT /evidence="ECO:0000305" FT CONFLICT 2769 FT /note="Missing (in Ref. 1; AAN46668)" FT /evidence="ECO:0000305" FT CONFLICT 2885 FT /note="Missing (in Ref. 1; AAN46668)" FT /evidence="ECO:0000305" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 53..67 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 71..77 FT /evidence="ECO:0007829|PDB:8B55" FT TURN 79..85 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 96..103 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 120..127 FT /evidence="ECO:0007829|PDB:8B55" FT TURN 128..131 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 140..146 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 179..190 FT /evidence="ECO:0007829|PDB:8B55" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:8B55" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:8B55" FT HELIX 2724..2726 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2740..2757 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2759..2762 FT /evidence="ECO:0007829|PDB:7WUJ" FT TURN 2763..2765 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2770..2772 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2775..2802 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2806..2837 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2849..2857 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2860..2871 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2873..2876 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2892..2895 FT /evidence="ECO:0007829|PDB:7WUJ" FT TURN 2896..2898 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2899..2924 FT /evidence="ECO:0007829|PDB:7WUJ" FT TURN 2932..2934 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2936..2942 FT /evidence="ECO:0007829|PDB:7WUJ" FT TURN 2943..2950 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2952..2954 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2955..2959 FT /evidence="ECO:0007829|PDB:7WUJ" FT STRAND 2961..2963 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2966..2974 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2978..2986 FT /evidence="ECO:0007829|PDB:7WUJ" FT TURN 2987..2990 FT /evidence="ECO:0007829|PDB:7WUJ" FT HELIX 2993..2997 FT /evidence="ECO:0007829|PDB:7WUJ" SQ SEQUENCE 3080 AA; 333368 MW; 3449BC820B251BD3 CRC64; MKEHIIYQKL YGLILMSSFI FLSDTLSLKG KKLDFFGRGD TYVSLIDTIP ELSRFTACID LVFMDDNSRY WMAFSYITNN ALLGREDIDL GLAGDHQQLI LYRLGKTFSI RHHLASFQWH TICLIWDGVK GKLELFLNKE RILEVTDQPH NLTPHGTLFL GHFLKNESSE VKSMMRSFPG SLYYFQLWDH ILENEEFMKC LDGNIVSWEE DVWLVNKIIP TVDRTLRCFV PENMTIQEKS TTVSQQIDMT TPSQITGVKP QNTAHSSTLL SQSIPIFATD YTTISYSNTT SPPLETMTAQ KILKTLVDET ATFAVDVLST SSAISLPTQS ISIDNTTNSM KKTKSPSSES TKTTKMVEAM ATEIFQPPTP SNFLSTSRFT KNSVVSTTSA IKSQSAVTKT TSLFSTIEST SMSTTPCLKQ KSTNTGALPI STAGQEFIES TAAGTVPWFT VEKTSPASTH VGTASSFPPE PVLISTAAPV DSVFPRNQTA FPLATTDMKI AFTVHSLTLP TRLIETTPAP RTAETELTST NFQDVSLPRV EDAMSTSMSK ETSSKTFSFL TSFSFTGTES VQTVIDAEAT RTALTPEITL ASTVAETMLS STITGRVYTQ NTPTADGHLL TLMSTRSAST SKAPESGPTS TTDEAAHLFS SNETIWTSRP DQALLASMNT TTILTFVPNE NFTSAFHENT TYTEYLSATT NITPLKASPE GKGTTANDAT TARYTTAVSK LTSPWFANFS IVSGTTSITN MPEFKLTTLL LKTIPMSTKP ANELPLTPRE TVVPSVDIIS TLACIQPNFS TEESASETTQ TEINGAIVFG GTTTPVPKSA TTQRLNATVT RKEATSHYLM RKSTIAAVAE VSPFSTMLEV TDESAQRVTA SVTVSSFPDI EKLSTPLDNK TATTEVRESW LLTKLVKTTP RSSYNEMTEM FNFNHTYVAH WTSETSEGIS AGSPTSGSTH IFGEPLGAST TRISETSFST TPTDRTATSL SDGILPPQPT AAHSSATPVP VTHMFSLPVN GSSVVAEETE VTMSEPSTLA RAFSTSVLSD VSNLSSTTMT TALVPPLDQT ASTTIVIVPT HGDLIRTTSE ATVISVRKTS MAVPSLTETP FHSLRLSTPV TAKAETTLFS TSVDTVTPST HTLVCSKPPP DNIPPASSTH VISTTSTPEA TQPISQVEET STYALSFPYT FSGGGVVASL ATGTTETSVV DETTPSHISA NKLTTSVNSH ISSSATYRVH TPVSIQLVTS TSVLSSDKDQ MTISLGKTPR TMEVTEMSPS KNSFISYSRG TPSLEMTDTG FPETTKISSH QTHSPSEIPL GTPSDGNLAS SPTSGSTQIT PTLTSSNTVG VHIPEMSTSL GKTALPSQAL TITTFLCPEK ESTSALPAYT PRTVEMIVNS TYVTHSVSYG QDTSFVDTTT SSSTRISNPM DINTTFSHLH SLRTQPEVTS VASFISESTQ TFPESLSLST AGLYNDGFTV LSDRITTAFS VPNVPTMLPR ESSMATSTPI YQMSSLPVNV TAFTSKKVSD TPPIVITKSS KTMHPGCLKS PCTATSGPMS EMSSIPVNNS AFTPATVSSD TSTRVGLFST LLSSVTPRTT MTMQTSTLDV TPVIYAGATS KNKMVSSAFT TEMIEAPSRI TPTTFLSPTE PTLPFVKTVP TTIMAGIVTP FVGTTAFSPL SSKSTGAISS IPKTTFSPFL SATQQSSQAD EATTLGILSG ITNRSLSTVN SGTGVALTDT YSRITVPENM LSPTHADSLH TSFNIQVSPS LTSFKSASGP TKNVKTTTNC FSSNTRKMTS LLEKTSLTNY ATSLNTPVSY PPWTPSSATL PSLTSFVYSP HSTEAEISTP KTSPPPTSQM VEFPVLGTRM TSSNTQPLLM TSWNIPTAEG SQFPISTTIN VPTSNEMETE TLHLVPGPLS TFTASQTGLV SKDVMAMSSI PMSGILPNHG LSENPSLSTS LRAITSTLAD VKHTFEKMTT SVTPGTTLPS ILSGATSGSV ISKSPILTWL LSSLPSGSPP ATVSNAPHVM TSSTVEVSKS TFLTSDMISA HPFTNLTTLP SATMSTILTR TIPTPTLGGI TTGFPTSLPM SINVTDDIVY ISTHPEASSR TTITANPRTV SHPSSFSRKT MSPSTTDHTL SVGAMPLPSS TITSSWNRIP TASSPSTLII PKPTLDSLLN IMTTTSTVPG ASFPLISTGV TYPFTATVSS PISSFFETTW LDSTPSFLST EASTSPTATK STVSFYNVEM SFSVFVEEPR IPITSVINEF TENSLNSIFQ NSEFSLATLE TQIKSRDISE EEMVMDRAIL EQREGQEMAT ISYVPYSCVC QVIIKASSSL ASSELMRKIK SKIHGNFTHG NFTQDQLTLL VNCEHVAVKK LEPGNCKADE TASKYKGTYK WLLTNPTETA QTRCIKNEDG NATRFCSISI NTGKSQWEKP KFKQCKLLQE LPDKIVDLAN ITISDENAED VAEHILNLIN ESPALGKEET KIIVSKISDI SQCDEISMNL THVMLQIINV VLEKQNNSAS DLHEISNEIL RIIERTGHKM EFSGQIANLT VAGLALAVLR GDHTFDGMAF SIHSYEEGTD PEIFLGNVPV GGILASIYLP KSLTERIPLS NLQTILFNFF GQTSLFKTKN VTKALTTYVV SASISDDMFI QNLADPVVIT LQHIGGNQNY GQVHCAFWDF ENNNGLGGWN SSGCKVKETN VNYTICQCDH LTHFGVLMDL SRSTVDSVNE QILALITYTG CGISSIFLGV AVVTYIAFHK LRKDYPAKIL INLCTALLML NLVFLINSWL SSFQKVGVCI TAAVALHYFL LVSFTWMGLE AVHMYLALVK VFNIYIPNYI LKFCLVGWGI PAIMVAITVS VKKDLYGTLS PTTPFCWIKD DSIFYISVVA YFCLIFLMNL SMFCTVLVQL NSVKSQIQKT RRKMILHDLK GTMSLTFLLG LTWGFAFFAW GPMRNFFLYL FAIFNTLQGF FIFVFHCVMK ESVREQWQIH LCCGWLRLDN SSDGSSRCQI KVGYKQEGLK KIFEHKLLTP SLKSTATSST FKSLGSAQGT PSEISFPNDD FDKDPYCSSP //