TPPC4_HUMAN
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 03-AUG-2022, entry version 181.
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 -!- INTERACTION:
CC Q9Y296; P28482: MAPK1; NbExp=3; IntAct=EBI-722888, EBI-959949;
CC Q9Y296; Q9CQA1: Trappc5; Xeno; NbExp=2; IntAct=EBI-722888, EBI-1172213;
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}.
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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_001318489.1. [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_016146.5. [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; 70.
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 IntAct; Q9Y296; 30.
DR STRING; 9606.ENSP00000436005; -.
DR DrugBank; DB08342; S-palmitoyl-L-cysteine.
DR iPTMnet; Q9Y296; -.
DR PhosphoSitePlus; Q9Y296; -.
DR BioMuta; TRAPPC4; -.
DR DMDM; 20178121; -.
DR EPD; Q9Y296; -.
DR jPOST; Q9Y296; -.
DR MassIVE; Q9Y296; -.
DR MaxQB; Q9Y296; -.
DR PaxDb; Q9Y296; -.
DR PeptideAtlas; Q9Y296; -.
DR PRIDE; Q9Y296; -.
DR ProteomicsDB; 4601; -.
DR ProteomicsDB; 85704; -. [Q9Y296-1]
DR Antibodypedia; 32564; 306 antibodies from 26 providers.
DR DNASU; 51399; -.
DR Ensembl; ENST00000434101.6; ENSP00000405033.2; ENSG00000196655.12. [Q9Y296-2]
DR Ensembl; ENST00000533632.6; ENSP00000436005.1; ENSG00000196655.12. [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 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 neXtProt; NX_Q9Y296; -.
DR OpenTargets; ENSG00000196655; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA134906910; -.
DR VEuPathDB; HostDB:ENSG00000196655; -.
DR eggNOG; KOG3369; Eukaryota.
DR GeneTree; ENSGT00940000153761; -.
DR InParanoid; Q9Y296; -.
DR OMA; GQRDGIN; -.
DR OrthoDB; 1504863at2759; -.
DR PhylomeDB; Q9Y296; -.
DR TreeFam; TF314561; -.
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 BioGRID-ORCS; 51399; 471 hits in 1083 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 99 other tissues.
DR ExpressionAtlas; Q9Y296; baseline and differential.
DR Genevisible; Q9Y296; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IC: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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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; IC:ComplexPortal.
DR GO; GO:1990072; C:TRAPPIII protein complex; IC:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; IC: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; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR DisProt; DP00562; -.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR007233; TRAPPC.
DR PANTHER; PTHR23249; PTHR23249; 1.
DR Pfam; PF04099; Sybindin; 1.
DR SMART; SM01399; Sybindin; 1.
DR SUPFAM; SSF64356; SSF64356; 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 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
