ID STEEP_HUMAN Reviewed; 222 AA. AC Q9H5V9; A8MPX7; B4DQN2; D3DWH9; F5GWL7; O43351; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=STING ER exit protein {ECO:0000303|PubMed:32690950}; DE Short=STEEP {ECO:0000303|PubMed:32690950}; GN Name=STEEP1 {ECO:0000312|HGNC:HGNC:26239}; GN Synonyms=CXorf56 {ECO:0000312|HGNC:HGNC:26239}; 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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] 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 [3] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] RP INVOLVEMENT IN XLID107, AND SUBCELLULAR LOCATION. RX PubMed=29374277; DOI=10.1038/s41431-017-0051-9; RA Verkerk A.J.M.H., Zeidler S., Breedveld G., Overbeek L., Huigh D., RA Koster L., van der Linde H., de Esch C., Severijnen L.A., de Vries B.B.A., RA Swagemakers S.M.A., Willemsen R., Hoogeboom A.J.M., van der Spek P.J., RA Oostra B.A.; RT "CXorf56, a dendritic neuronal protein, identified as a new candidate gene RT for X-linked intellectual disability."; RL Eur. J. Hum. Genet. 26:552-560(2018). RN [7] RP FUNCTION, INTERACTION WITH STING1; PIK3C3 AND ATG14, SUBCELLULAR LOCATION, RP MUTAGENESIS OF 149-LYS--TYR-178, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=32690950; DOI=10.1038/s41590-020-0730-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RT "STEEP mediates STING ER exit and activation of signaling."; RL Nat. Immunol. 21:868-879(2020). RN [8] RP ERRATUM OF PUBMED:32690950. RX PubMed=32929276; DOI=10.1038/s41590-020-0803-5; RA Zhang B.C., Nandakumar R., Reinert L.S., Huang J., Laustsen A., Gao Z.L., RA Sun C.L., Jensen S.B., Troldborg A., Assil S., Berthelsen M.F., RA Scavenius C., Zhang Y., Windross S.J., Olagnier D., Prabakaran T., RA Bodda C., Narita R., Cai Y., Zhang C.G., Stenmark H., Doucet C.M., Noda T., RA Guo Z., Goldbach-Mansky R., Hartmann R., Chen Z.J., Enghild J.J., Bak R.O., RA Thomsen M.K., Paludan S.R.; RL Nat. Immunol. 21:1468-1469(2020). RN [9] RP FUNCTION, AND INTERACTION WITH STING1. RX PubMed=37832545; DOI=10.1016/j.molcel.2023.09.009; RA Ma M., Dang Y., Chang B., Wang F., Xu J., Chen L., Su H., Li J., Ge B., RA Chen C., Liu H.; RT "TAK1 is an essential kinase for STING trafficking."; RL Mol. Cell 0:0-0(2023). CC -!- FUNCTION: Molecular adapter that stimulates membrane curvature CC formation and subsequent endoplasmic reticulum exit site (ERES) CC establishment by recruiting PI3K complex I, leading to COPII vesicle- CC mediated transport (PubMed:32690950). Promotes endoplasmic reticulum CC (ER) exit of cGAMP-activated STING1 oligomers (PubMed:32690950, CC PubMed:37832545). {ECO:0000269|PubMed:32690950, CC ECO:0000269|PubMed:37832545}. CC -!- SUBUNIT: Interacts with STING1; interaction takes place upon cGAMP- CC activation and STING1 phosphorylation by MAP3K7/TAK1 and leads to CC recruitment of PI3K complex I (PubMed:32690950, PubMed:37832545). CC Interacts with PIK3C3; the STING1-STEEP1 interaction leads to CC recruitment of PI3K complex I (PubMed:32690950, PubMed:37832545). CC Interacts with ATG14 (PubMed:32690950). {ECO:0000269|PubMed:32690950, CC ECO:0000269|PubMed:37832545}. CC -!- INTERACTION: CC Q9H5V9; O14929: HAT1; NbExp=3; IntAct=EBI-1053419, EBI-2339359; CC Q9H5V9; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-1053419, EBI-8472129; CC Q9H5V9; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-1053419, EBI-14066006; CC Q9H5V9; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-1053419, EBI-747925; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32690950}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:32690950}; CC Peripheral membrane protein {ECO:0000269|PubMed:32690950}; Cytoplasmic CC side {ECO:0000269|PubMed:32690950}. Nucleus CC {ECO:0000269|PubMed:29374277, ECO:0000269|PubMed:32690950}. CC Note=Recruited to the endoplasmic reticulum following interaction with CC phosphorylated STING1. {ECO:0000269|PubMed:37832545}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H5V9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H5V9-2; Sequence=VSP_044273; CC Name=3; CC IsoId=Q9H5V9-3; Sequence=VSP_044274; CC -!- DISEASE: Intellectual developmental disorder, X-linked 107 (XLID107) CC [MIM:301013]: A form of intellectual disability, a disorder CC characterized by significantly below average general intellectual CC functioning associated with impairments in adaptive behavior and CC manifested during the developmental period. Intellectual deficiency is CC the only primary symptom of non-syndromic X-linked forms, while CC syndromic forms present with associated physical, neurological and/or CC psychiatric manifestations. {ECO:0000269|PubMed:29374277}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the STEEP1 family. {ECO:0000305}. CC -!- CAUTION: May be duplicated on chromosome 8, within an intron of the CC ERLIN2 gene. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB96348.1; Type=Erroneous gene model prediction; 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; AK026618; BAB15510.1; -; mRNA. DR EMBL; AK298877; BAG60994.1; -; mRNA. DR EMBL; AK096297; BAG53251.1; -; mRNA. DR EMBL; AC004000; AAB96348.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC004913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005190; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471161; EAW89864.1; -; Genomic_DNA. DR EMBL; CH471161; EAW89865.1; -; Genomic_DNA. DR EMBL; CH471161; EAW89866.1; -; Genomic_DNA. DR EMBL; CH471161; EAW89867.1; -; Genomic_DNA. DR EMBL; BC023506; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS55484.1; -. [Q9H5V9-2] DR CCDS; CCDS55485.1; -. [Q9H5V9-3] DR CCDS; CCDS94660.1; -. [Q9H5V9-1] DR RefSeq; NP_001164040.1; NM_001170569.1. [Q9H5V9-2] DR RefSeq; NP_001164041.1; NM_001170570.1. [Q9H5V9-3] DR RefSeq; NP_071384.1; NM_022101.3. [Q9H5V9-1] DR PDB; 8C6J; EM; 2.80 A; j=1-222. DR PDBsum; 8C6J; -. DR AlphaFoldDB; Q9H5V9; -. DR EMDB; EMD-16452; -. DR SMR; Q9H5V9; -. DR BioGRID; 122000; 71. DR IntAct; Q9H5V9; 16. DR MINT; Q9H5V9; -. DR STRING; 9606.ENSP00000441786; -. DR GlyGen; Q9H5V9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H5V9; -. DR PhosphoSitePlus; Q9H5V9; -. DR BioMuta; CXorf56; -. DR DMDM; 74733589; -. DR EPD; Q9H5V9; -. DR jPOST; Q9H5V9; -. DR MassIVE; Q9H5V9; -. DR MaxQB; Q9H5V9; -. DR PaxDb; 9606-ENSP00000441786; -. DR PeptideAtlas; Q9H5V9; -. DR ProteomicsDB; 1920; -. DR ProteomicsDB; 24155; -. DR ProteomicsDB; 80936; -. [Q9H5V9-1] DR Pumba; Q9H5V9; -. DR Antibodypedia; 50191; 100 antibodies from 18 providers. DR DNASU; 63932; -. DR Ensembl; ENST00000320339.8; ENSP00000320345.4; ENSG00000018610.15. [Q9H5V9-2] DR Ensembl; ENST00000536133.2; ENSP00000441786.1; ENSG00000018610.15. [Q9H5V9-3] DR Ensembl; ENST00000644802.2; ENSP00000494123.2; ENSG00000018610.15. [Q9H5V9-1] DR GeneID; 63932; -. DR KEGG; hsa:63932; -. DR MANE-Select; ENST00000644802.2; ENSP00000494123.2; NM_022101.4; NP_071384.1. DR UCSC; uc004erj.3; human. [Q9H5V9-1] DR AGR; HGNC:26239; -. DR CTD; 63932; -. DR DisGeNET; 63932; -. DR GeneCards; STEEP1; -. DR HGNC; HGNC:26239; STEEP1. DR HPA; ENSG00000018610; Low tissue specificity. DR MalaCards; STEEP1; -. DR MIM; 301012; gene. DR MIM; 301013; phenotype. DR neXtProt; NX_Q9H5V9; -. DR OpenTargets; ENSG00000018610; -. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000018610; -. DR eggNOG; KOG4397; Eukaryota. DR GeneTree; ENSGT00390000002197; -. DR HOGENOM; CLU_099571_1_1_1; -. DR InParanoid; Q9H5V9; -. DR OMA; HVTFVMF; -. DR OrthoDB; 2874101at2759; -. DR PhylomeDB; Q9H5V9; -. DR TreeFam; TF300272; -. DR PathwayCommons; Q9H5V9; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q9H5V9; -. DR BioGRID-ORCS; 63932; 66 hits in 774 CRISPR screens. DR ChiTaRS; CXorf56; human. DR GenomeRNAi; 63932; -. DR Pharos; Q9H5V9; Tdark. DR PRO; PR:Q9H5V9; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9H5V9; Protein. DR Bgee; ENSG00000018610; Expressed in oocyte and 170 other cell types or tissues. DR GO; GO:0044297; C:cell body; ISS:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB. DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IDA:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB. DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IDA:UniProtKB. DR InterPro; IPR029704; STEEP-like. DR PANTHER; PTHR46355:SF1; STING ER EXIT PROTEIN; 1. DR PANTHER; PTHR46355; UPF0428 PROTEIN CXORF56; 1. DR Genevisible; Q9H5V9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; KW Endoplasmic reticulum; Intellectual disability; Membrane; Nucleus; KW Reference proteome. FT CHAIN 1..222 FT /note="STING ER exit protein" FT /id="PRO_0000287609" FT COILED 170..220 FT /evidence="ECO:0000255" FT VAR_SEQ 1..49 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044273" FT VAR_SEQ 82..95 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044274" FT MUTAGEN 149..178 FT /note="KDMGKFSSVTVSTIDEEEEEIEAREVADSY->ADMAKFSSVTVSTIDEEAEA FT IEAREVADSA: Abrogates interaction with STING1 and impairs FT STING1-mediated signaling." FT /evidence="ECO:0000269|PubMed:32690950" FT CONFLICT 194 FT /note="M -> V (in Ref. 1; BAG60994)" FT /evidence="ECO:0000305" SQ SEQUENCE 222 AA; 25625 MW; 586CD0CE472989DF CRC64; MPKVVSRSVV CSDTRDREEY DDGEKPLHVY YCLCGQMVLV LDCQLEKLPM RPRDRSRVID AAKHAHKFCN TEDEETMYLR RPEGIERQYR KKCAKCGLPL FYQSQPKNAP VTFIVDGAVV KFGQGFGKTN IYTQKQEPPK KVMMTKRTKD MGKFSSVTVS TIDEEEEEIE AREVADSYAQ NAKVIEKQLE RKGMSKRRLQ ELAELEAKKA KMKGTLIDNQ FK //