GORS2_MOUSE
ID GORS2_MOUSE Reviewed; 451 AA.
AC Q99JX3; Q3U9D2; Q8CCD0; Q91W68;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Golgi reassembly-stacking protein 2;
DE Short=GRS2;
DE AltName: Full=Golgi reassembly-stacking protein of 55 kDa;
DE Short=GRASP55 {ECO:0000303|PubMed:10487747};
GN Name=Gorasp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10487747; DOI=10.1093/emboj/18.18.4949;
RA Shorter J., Watson R., Giannakou M.-E., Clarke M., Warren G., Barr F.A.;
RT "GRASP55, a second mammalian GRASP protein involved in the stacking of
RT Golgi cisternae in a cell-free system.";
RL EMBO J. 18:4949-4960(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Mammary tumor;
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 [4]
RP INTERACTION WITH BLZF1, AND SUBUNIT.
RX PubMed=11739401; DOI=10.1083/jcb.200108079;
RA Short B., Preisinger C., Koerner R., Kopajtich R., Byron O., Barr F.A.;
RT "A GRASP55-rab2 effector complex linking Golgi structure to membrane
RT traffic.";
RL J. Cell Biol. 155:877-883(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-443, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7] {ECO:0007744|PDB:5GML}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-208.
RA Cartier-Michaud A., Betzi S., Shi X., Shi N., Morelli X., Aurrand-Lions M.;
RT "Structural relationship of the tandem PDZ tandem from Grasp55 and its
RT implication in the unconventional secretion pathway.";
RL Submitted (JUL-2016) to the PDB data bank.
RN [8] {ECO:0007744|PDB:5H3J}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 2-208 IN COMPLEX WITH BLZF1
RP PEPTIDE, AND MUTAGENESIS OF GLY-97 AND ARG-101.
RX PubMed=28049725; DOI=10.1074/jbc.m116.765990;
RA Zhao J., Li B., Huang X., Morelli X., Shi N.;
RT "Structural Basis for the Interaction between Golgi Reassembly-stacking
RT Protein GRASP55 and Golgin45.";
RL J. Biol. Chem. 292:2956-2965(2017).
RN [9] {ECO:0007744|PDB:5GMI, ECO:0007744|PDB:5GMJ}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 2-208 IN COMPLEXES WITH JAM2 AND
RP JAM3, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE,
RP AND TISSUE SPECIFICITY.
RX PubMed=28617811; DOI=10.1371/journal.pgen.1006803;
RA Cartier-Michaud A., Bailly A.L., Betzi S., Shi X., Lissitzky J.C.,
RA Zarubica A., Serge A., Roche P., Lugari A., Hamon V., Bardin F.,
RA Derviaux C., Lembo F., Audebert S., Marchetto S., Durand B., Borg J.P.,
RA Shi N., Morelli X., Aurrand-Lions M.;
RT "Genetic, structural, and chemical insights into the dual function of
RT GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization
RT during spermatogenesis.";
RL PLoS Genet. 13:e1006803-e1006803(2017).
CC -!- FUNCTION: Plays a role in assembly and membrane stacking of the Golgi
CC cisternae, and in the process by which Golgi stacks reform after
CC breakdown during mitosis and meiosis (PubMed:28617811). May regulate
CC the intracellular transport and presentation of a defined set of
CC transmembrane proteins, such as transmembrane TGFA (By similarity).
CC Required for normal acrosome formation during spermiogenesis and normal
CC male fertility, probably by promoting colocalization of JAM2 and JAM3
CC at contact sites between germ cells and Sertoli cells
CC (PubMed:28617811). Mediates ER stress-induced unconventional (ER/Golgi-
CC independent) trafficking of core-glycosylated CFTR to cell membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q9H8Y8,
CC ECO:0000269|PubMed:28617811}.
CC -!- SUBUNIT: Homodimer. Homooligomer. ER stress induces phosphorylation-
CC dependent monomerization (By similarity). Interacts with BLZF1/Golgin
CC 45 (PubMed:11739401, PubMed:28049725). Identified in a complex with
CC RAB2 and GORASP2 (PubMed:11739401). Interacts with JAM2 and JAM3
CC (PubMed:28617811). Interacts with members of the p24 cargo receptors.
CC Interacts with CNIH and the cytoplasmic domain of transmembrane TGFA,
CC prior its transit in the trans-Golgi. Interacts with KCTD5 (By
CC similarity). Interacts with TMED2 and TMED3 (By similarity). Interacts
CC with SEC16A in response to ER stress (By similarity). Interacts (via
CC PDZ GRASP-type 1 domain) with core-glycosylated CFTR in response to ER
CC stress (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8,
CC ECO:0000250|UniProtKB:Q9R064, ECO:0000269|PubMed:11739401,
CC ECO:0000269|PubMed:28049725, ECO:0000269|PubMed:28617811}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9R064}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9R064}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H8Y8}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9H8Y8}. Note=Detected in the intermediate
CC Golgi, membrane-associated. ER stress triggers its relocalization from
CC Golgi to ER membrane. {ECO:0000250|UniProtKB:Q9H8Y8,
CC ECO:0000250|UniProtKB:Q9R064}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99JX3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99JX3-2; Sequence=VSP_011301;
CC -!- TISSUE SPECIFICITY: Detected in lung, heart and testis. Colocalized in
CC a polarized fashion in the acrosome region with JAM3 in round
CC spermatids (at protein level). {ECO:0000269|PubMed:28617811}.
CC -!- PTM: Myristoylated (By similarity). Myristoylation is essential for the
CC Golgi targeting (By similarity). {ECO:0000250|UniProtKB:Q9H8Y8,
CC ECO:0000250|UniProtKB:Q9R064}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q9H8Y8}.
CC -!- PTM: Phosphorylated in mitotic cells. ER stress-induced phosphorylation
CC at Ser-443 induces monomerization and subsequent relocalization from
CC Golgi to ER which is essential for mediating unconventional (ER/Golgi-
CC independent) trafficking of CFTR to the cell membrane.
CC {ECO:0000250|UniProtKB:Q9H8Y8}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice have normal weight at birth, but
CC display growth retardation and lower body weight during postnatal
CC development and in adulthood. Females display normal fertility. Males
CC have normal mating behavior, but are infertile, due to defects in
CC spermiogenesis and acrosome formation. {ECO:0000269|PubMed:28617811}.
CC -!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
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DR EMBL; AK033413; BAC28276.1; -; mRNA.
DR EMBL; AK077683; BAC36954.1; -; mRNA.
DR EMBL; AK077706; BAC36969.1; -; mRNA.
DR EMBL; AK148337; BAE28492.1; -; mRNA.
DR EMBL; AK151843; BAE30735.1; -; mRNA.
DR EMBL; AK152475; BAE31249.1; -; mRNA.
DR EMBL; AK152544; BAE31299.1; -; mRNA.
DR EMBL; AK152603; BAE31351.1; -; mRNA.
DR EMBL; AK153049; BAE31677.1; -; mRNA.
DR EMBL; AK169382; BAE41129.1; -; mRNA.
DR EMBL; BC005600; AAH05600.1; -; mRNA.
DR EMBL; BC016455; AAH16455.1; -; mRNA.
DR CCDS; CCDS16109.1; -. [Q99JX3-1]
DR RefSeq; NP_081628.3; NM_027352.4. [Q99JX3-1]
DR PDB; 5GMI; X-ray; 2.71 A; A/B=2-208.
DR PDB; 5GMJ; X-ray; 2.99 A; A/B=2-208.
DR PDB; 5GML; X-ray; 2.55 A; A/B=2-208.
DR PDB; 5H3J; X-ray; 1.33 A; A=2-208.
DR PDBsum; 5GMI; -.
DR PDBsum; 5GMJ; -.
DR PDBsum; 5GML; -.
DR PDBsum; 5H3J; -.
DR AlphaFoldDB; Q99JX3; -.
DR SMR; Q99JX3; -.
DR BioGRID; 213929; 23.
DR STRING; 10090.ENSMUSP00000028509; -.
DR TCDB; 9.A.48.1.1; the unconventional protein secretion (ups) system.
DR iPTMnet; Q99JX3; -.
DR PhosphoSitePlus; Q99JX3; -.
DR EPD; Q99JX3; -.
DR jPOST; Q99JX3; -.
DR MaxQB; Q99JX3; -.
DR PaxDb; Q99JX3; -.
DR PeptideAtlas; Q99JX3; -.
DR PRIDE; Q99JX3; -.
DR ProteomicsDB; 267743; -. [Q99JX3-1]
DR ProteomicsDB; 267744; -. [Q99JX3-2]
DR Antibodypedia; 33839; 311 antibodies from 31 providers.
DR DNASU; 70231; -.
DR Ensembl; ENSMUST00000028509; ENSMUSP00000028509; ENSMUSG00000014959. [Q99JX3-1]
DR GeneID; 70231; -.
DR KEGG; mmu:70231; -.
DR UCSC; uc008jzo.2; mouse. [Q99JX3-1]
DR CTD; 26003; -.
DR MGI; MGI:2135962; Gorasp2.
DR VEuPathDB; HostDB:ENSMUSG00000014959; -.
DR eggNOG; KOG3834; Eukaryota.
DR GeneTree; ENSGT00390000008686; -.
DR InParanoid; Q99JX3; -.
DR OMA; HIVPEMV; -.
DR OrthoDB; 1366434at2759; -.
DR PhylomeDB; Q99JX3; -.
DR TreeFam; TF314053; -.
DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR BioGRID-ORCS; 70231; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Gorasp2; mouse.
DR PRO; PR:Q99JX3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99JX3; protein.
DR Bgee; ENSMUSG00000014959; Expressed in ileal epithelium and 257 other tissues.
DR ExpressionAtlas; Q99JX3; baseline and differential.
DR Genevisible; Q99JX3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0070925; P:organelle assembly; ISO:MGI.
DR GO; GO:0006996; P:organelle organization; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR007583; GRASP55_65.
DR InterPro; IPR024958; GRASP_PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12893; PTHR12893; 1.
DR Pfam; PF04495; GRASP55_65; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS51865; PDZ_GRASP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Differentiation; Endoplasmic reticulum;
KW Golgi apparatus; Lipoprotein; Membrane; Methylation; Myristate; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT CHAIN 2..451
FT /note="Golgi reassembly-stacking protein 2"
FT /id="PRO_0000087546"
FT DOMAIN 15..105
FT /note="PDZ GRASP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT DOMAIN 111..199
FT /note="PDZ GRASP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT REGION 15..215
FT /note="GRASP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT REGION 194..199
FT /note="Important for membrane binding"
FT /evidence="ECO:0000250"
FT REGION 236..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9R064"
FT MOD_RES 47
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9R064"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 225
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y8"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011301"
FT MUTAGEN 97
FT /note="G->D: Reduced interaction with BLZF1."
FT /evidence="ECO:0000269|PubMed:28049725"
FT MUTAGEN 101
FT /note="R->A: No significant effect on interaction with
FT BLZF1."
FT /evidence="ECO:0000269|PubMed:28049725"
FT CONFLICT 93
FT /note="Q -> L (in Ref. 3; AAH16455)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="P -> L (in Ref. 2; BAC28276)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5GMJ"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:5H3J"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:5H3J"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5H3J"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:5H3J"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:5H3J"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:5H3J"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:5H3J"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:5H3J"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5GMJ"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:5H3J"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:5H3J"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5H3J"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5H3J"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5GMI"
SQ SEQUENCE 451 AA; 47038 MW; 7E37234E827B459A CRC64;
MGSSQSVEIP GGGTEGYHVL RVQENSPGHR AGLEPFFDFI VSINGSRLNK DNDTLKDLLK
ANVEKPVKML IYSSKTLELR EASVTPSNLW GGQGLLGVSI RFCSFDGANE NVWHVLEVES
NSPAALAGLR PHSDYIIGAD TVMNESEDLF SLIETHEAKP LKLYVYNTDT DNCREVIITP
NSAWGGEGSL GCGIGYGYLH RIPTRPFEEG KKISLPGQMT GTPITPLKDG FTEVQLSSVS
PPSLSPPGTT GVEQSLSGLS ISSAPPAVSN VLSTGVPTVP LLPPQVNQSL ASMPPMNPAT
TLPSLMPLSA GLPSLPNLPS LSNFNLPAPH IMPGVGLPEL GSPGLPPLPS LPPRNLPGIA
PLPMLSDFLP SFPLVPEGSS AASAGEPLSS LPAMGPPSDP VMTTAKADAS SLTVDVTSPA
SKVPTTVEDR VSDCTPAVEK PVSDADASEP S
