ID TPPC4_HUMAN Reviewed; 219 AA. AC Q9Y296; A8K3A5; B4DME1; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 28-JAN-2026, entry version 196. DE RecName: Full=Trafficking protein particle complex subunit 4 {ECO:0000305}; DE AltName: Full=Hematopoietic stem/progenitor cell protein 172; DE AltName: Full=Synbindin {ECO:0000250|UniProtKB:Q9ES56}; DE AltName: Full=TRS23 homolog; GN Name=TRAPPC4 {ECO:0000312|HGNC:HGNC:19943}; GN Synonyms=SBDN {ECO:0000250|UniProtKB:Q9ES56}; GN ORFNames=CGI-104, HSPC172, PTD009; 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). RC TISSUE=Brain; RA Zhu X., Zhao X.; RT "Human unknown mRNA highly conserved among eukaryotes."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pituitary tumor; RA Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; 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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [9] RP IDENTIFICATION IN TRAPP COMPLEX. RX PubMed=11805826; DOI=10.1038/415141a; RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A., RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C., RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M., RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C., RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V., RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B., RA Neubauer G., Superti-Furga G.; RT "Functional organization of the yeast proteome by systematic analysis of RT protein complexes."; RL Nature 415:141-147(2002). RN [10] RP IDENTIFICATION IN TRAPP COMPLEX, AND INTERACTION WITH TRAPPC2L. RX PubMed=19416478; DOI=10.1111/j.1600-0854.2009.00906.x; RA Scrivens P.J., Shahrzad N., Moores A., Morin A., Brunet S., Sacher M.; RT "TRAPPC2L is a novel, highly conserved TRAPP-interacting protein."; RL Traffic 10:724-736(2009). RN [11] 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 [12] RP IDENTIFICATION IN TRAPP COMPLEX. RX PubMed=21525244; DOI=10.1091/mbc.e10-11-0873; RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.; RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early RT stage in ER-to-Golgi trafficking."; RL Mol. Biol. Cell 22:2083-2093(2011). RN [13] RP INVOLVEMENT IN NEDESBA, FUNCTION, AND IDENTIFICATION IN TRAPP COMPLEX. RX PubMed=31794024; DOI=10.1093/brain/awz374; RA Van Bergen N.J., Guo Y., Al-Deri N., Lipatova Z., Stanga D., Zhao S., RA Murtazina R., Gyurkovska V., Pehlivan D., Mitani T., Gezdirici A., RA Antony J., Collins F., Willis M.J.H., Coban Akdemir Z.H., Liu P., RA Punetha J., Hunter J.V., Jhangiani S.N., Fatih J.M., Rosenfeld J.A., RA Posey J.E., Gibbs R.A., Karaca E., Massey S., Ranasinghe T.G., Sleiman P., RA Troedson C., Lupski J.R., Sacher M., Segev N., Hakonarson H., RA Christodoulou J.; RT "Deficiencies in vesicular transport mediated by TRAPPC4 are associated RT with severe syndromic intellectual disability."; RL Brain 143:112-130(2020). CC -!- FUNCTION: Core component of the TRAPP complexes which has a function of CC guanine nucleotide exchange factor activity for Rab1 GTPase (Probable). CC Plays a role in vesicular transport from endoplasmic reticulum to Golgi CC and autophagy (PubMed:31794024). May play a role in dendrite CC postsynaptic membrane trafficking (By similarity). CC {ECO:0000250|UniProtKB:Q9ES56, ECO:0000269|PubMed:31794024, CC ECO:0000305|PubMed:31794024}. CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3, CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and CC TRAPPC12 (Probable). Interacts with SDC2 (By similarity). CC {ECO:0000250|UniProtKB:Q9ES56, ECO:0000305|PubMed:31794024}. CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:Q9ES56}. Golgi apparatus membrane CC {ECO:0000250|UniProtKB:Q9ES56}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q9ES56}. Vesicle {ECO:0000250|UniProtKB:Q9ES56}. CC Note=Associated with postsynaptic membranes and in intracellular CC cisterns and vesicles (Golgi). {ECO:0000250|UniProtKB:Q9ES56}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y296-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y296-2; Sequence=VSP_056348; CC -!- DISEASE: Neurodevelopmental disorder with epilepsy, spasticity, and CC brain atrophy (NEDESBA) [MIM:618741]: An autosomal recessive disorder CC characterized by severely impaired global development apparent soon CC after birth, early-onset seizures, lack of psychomotor development, CC spastic quadriparesis, progressive cortical and cerebellar atrophy, and CC dysmorphic features, including microcephaly. Death in childhood may CC occur. {ECO:0000269|PubMed:31794024}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4 CC 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; AF105025; AAF21897.1; -; mRNA. DR EMBL; AF078862; AAD44494.1; -; mRNA. DR EMBL; AF161520; AAF29135.1; -; mRNA. DR EMBL; AF151862; AAD34099.1; -; mRNA. DR EMBL; AK290520; BAF83209.1; -; mRNA. DR EMBL; AK297422; BAG59853.1; -; mRNA. DR EMBL; AP003392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67430.1; -; Genomic_DNA. DR EMBL; BC010866; AAH10866.1; -; mRNA. DR CCDS; CCDS81633.1; -. [Q9Y296-2] DR CCDS; CCDS8407.1; -. [Q9Y296-1] DR RefSeq; NP_001305415.1; NM_001318486.1. DR RefSeq; NP_001305417.1; NM_001318488.1. DR RefSeq; NP_001305418.1; NM_001318489.2. [Q9Y296-2] DR RefSeq; NP_001305419.1; NM_001318490.1. DR RefSeq; NP_001305421.1; NM_001318492.1. DR RefSeq; NP_001305423.1; NM_001318494.1. DR RefSeq; NP_057230.1; NM_016146.6. [Q9Y296-1] DR PDB; 2J3T; X-ray; 2.40 A; D=1-219. DR PDB; 2JSN; NMR; -; A=19-106. DR PDB; 2ZMV; X-ray; 2.80 A; A/B=1-219. DR PDBsum; 2J3T; -. DR PDBsum; 2JSN; -. DR PDBsum; 2ZMV; -. DR AlphaFoldDB; Q9Y296; -. DR BMRB; Q9Y296; -. DR SMR; Q9Y296; -. DR BioGRID; 119523; 85. DR ComplexPortal; CPX-4749; TRAPP II complex, TRAPPC2 variant. DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant. DR ComplexPortal; CPX-6902; TRAPP II complex, TRAPPC2B variant. DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant. DR CORUM; Q9Y296; -. DR DIP; DIP-37871N; -. DR FunCoup; Q9Y296; 1110. DR STRING; 9606.ENSP00000436005; -. DR DrugBank; DB08342; S-palmitoyl-L-cysteine. DR iPTMnet; Q9Y296; -. DR PhosphoSitePlus; Q9Y296; -. DR BioMuta; TRAPPC4; -. DR DMDM; 20178121; -. DR jPOST; Q9Y296; -. DR MassIVE; Q9Y296; -. DR PaxDb; 9606-ENSP00000436005; -. DR PeptideAtlas; Q9Y296; -. DR ProteomicsDB; 4601; -. DR ProteomicsDB; 85704; -. [Q9Y296-1] DR Pumba; Q9Y296; -. DR Antibodypedia; 32564; 311 antibodies from 26 providers. DR DNASU; 51399; -. DR Ensembl; ENST00000434101.6; ENSP00000405033.2; ENSG00000196655.13. [Q9Y296-2] DR Ensembl; ENST00000533632.6; ENSP00000436005.1; ENSG00000196655.13. [Q9Y296-1] DR Ensembl; ENST00000629243.3; ENSP00000487467.1; ENSG00000280495.5. [Q9Y296-1] DR Ensembl; ENST00000629713.2; ENSP00000486496.1; ENSG00000280495.5. [Q9Y296-2] DR GeneID; 51399; -. DR KEGG; hsa:51399; -. DR MANE-Select; ENST00000533632.6; ENSP00000436005.1; NM_016146.6; NP_057230.1. DR UCSC; uc010ryo.4; human. [Q9Y296-1] DR AGR; HGNC:19943; -. DR ClinPGx; PA134906910; -. DR CTD; 51399; -. DR DisGeNET; 51399; -. DR GeneCards; TRAPPC4; -. DR HGNC; HGNC:19943; TRAPPC4. DR HPA; ENSG00000196655; Low tissue specificity. DR MalaCards; TRAPPC4; -. DR MIM; 610971; gene. DR MIM; 618741; phenotype. DR OpenTargets; ENSG00000196655; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000196655; -. DR eggNOG; KOG3369; Eukaryota. DR GeneTree; ENSGT00940000153761; -. DR InParanoid; Q9Y296; -. DR OMA; GQRDGIN; -. DR OrthoDB; 246406at2759; -. DR PAN-GO; Q9Y296; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9Y296; -. DR PathwayCommons; Q9Y296; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR SignaLink; Q9Y296; -. DR Agora; ENSG00000196655; -. DR BioGRID-ORCS; 51399; 503 hits in 1161 CRISPR screens. DR ChiTaRS; TRAPPC4; human. DR EvolutionaryTrace; Q9Y296; -. DR GeneWiki; TRAPPC4; -. DR GenomeRNAi; 51399; -. DR Pharos; Q9Y296; Tbio. DR PRO; PR:Q9Y296; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9Y296; protein. DR Bgee; ENSG00000196655; Expressed in cortical plate and 101 other cell types or tissues. DR ExpressionAtlas; Q9Y296; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB. DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl. DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB. DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB. DR GO; GO:1990071; C:TRAPPII protein complex; NAS:ComplexPortal. DR GO; GO:1990072; C:TRAPPIII protein complex; NAS:ComplexPortal. DR GO; GO:0006914; P:autophagy; IMP:UniProtKB. DR GO; GO:0048208; P:COPII vesicle coating; NAS:ComplexPortal. DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB. DR GO; GO:0006901; P:vesicle coating; NAS:ComplexPortal. DR GO; GO:0099022; P:vesicle tethering; NAS:ComplexPortal. DR CDD; cd14856; TRAPPC4_synbindin; 1. DR DisProt; DP00562; -. DR FunFam; 3.30.450.70:FF:000002; Trafficking protein particle complex subunit 4; 1. DR Gene3D; 3.30.450.70; -; 1. DR InterPro; IPR011012; Longin-like_dom_sf. DR InterPro; IPR007233; TRAPPC. DR PANTHER; PTHR23249; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT; 1. DR PANTHER; PTHR23249:SF15; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 4; 1. DR Pfam; PF04099; Sybindin; 1. DR SMART; SM01399; Sybindin; 1. DR SUPFAM; SSF64356; SNARE-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Endoplasmic reticulum; KW ER-Golgi transport; Golgi apparatus; Membrane; Postsynaptic cell membrane; KW Proteomics identification; Reference proteome; Synapse; Transport. FT CHAIN 1..219 FT /note="Trafficking protein particle complex subunit 4" FT /id="PRO_0000211569" FT VAR_SEQ 81..134 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056348" FT VARIANT 78 FT /note="D -> A (in dbSNP:rs11640)" FT /id="VAR_052397" FT STRAND 3..9 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 44..51 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:2JSN" FT TURN 57..60 FT /evidence="ECO:0007829|PDB:2JSN" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:2J3T" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:2J3T" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:2J3T" FT HELIX 105..124 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:2J3T" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:2J3T" FT HELIX 166..181 FT /evidence="ECO:0007829|PDB:2J3T" FT HELIX 196..209 FT /evidence="ECO:0007829|PDB:2J3T" SQ SEQUENCE 219 AA; 24340 MW; C6ADE525B7CFB731 CRC64; MAIFSVYVVN KAGGLIYQLD SYAPRAEAEK TFSYPLDLLL KLHDERVLVA FGQRDGIRVG HAVLAINGMD VNGRYTADGK EVLEYLGNPA NYPVSIRFGR PRLTSNEKLM LASMFHSLFA IGSQLSPEQG SSGIEMLETD TFKLHCYQTL TGIKFVVLAD PRQAGIDSLL RKIYEIYSDF ALKNPFYSLE MPIRCELFDQ NLKLALEVAE KAGTFGPGS //