SPCS1_HUMAN
ID SPCS1_HUMAN Reviewed; 169 AA.
AC Q9Y6A9; B3KNF8; Q9BVW1; X6R2S6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 5.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Signal peptidase complex subunit 1;
DE AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE Short=SPase 12 kDa subunit;
GN Name=SPCS1; Synonyms=SPC12; ORFNames=HSPC033;
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-169.
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] OF 23-169.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-169, AND TOPOLOGY.
RX PubMed=8632014; DOI=10.1074/jbc.271.7.3925;
RA Kalies K.-U., Hartmann E.;
RT "Membrane topology of the 12- and the 25-kDa subunits of the mammalian
RT signal peptidase complex.";
RL J. Biol. Chem. 271:3925-3929(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-169.
RC TISSUE=Cervix;
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP TRANSLATION INITIATION SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24023390; DOI=10.1074/mcp.m113.030114;
RA Catherman A.D., Durbin K.R., Ahlf D.R., Early B.P., Fellers R.T.,
RA Tran J.C., Thomas P.M., Kelleher N.L.;
RT "Large-scale top down proteomics of the human proteome: membrane proteins,
RT mitochondria, and senescence.";
RL Mol. Cell. Proteomics 12:3465-3473(2013).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCV NS2 AND HCV E2
RP (MICROBIAL INFECTION).
RX PubMed=24009510; DOI=10.1371/journal.ppat.1003589;
RA Suzuki R., Matsuda M., Watashi K., Aizaki H., Matsuura Y., Wakita T.,
RA Suzuki T.;
RT "Signal peptidase complex subunit 1 participates in the assembly of
RT hepatitis C virus through an interaction with E2 and NS2.";
RL PLoS Pathog. 9:E1003589-E1003589(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=27383988; DOI=10.1038/nature18625;
RA Zhang R., Miner J.J., Gorman M.J., Rausch K., Ramage H., White J.P.,
RA Zuiani A., Zhang P., Fernandez E., Zhang Q., Dowd K.A., Pierson T.C.,
RA Cherry S., Diamond M.S.;
RT "A CRISPR screen defines a signal peptide processing pathway required by
RT flaviviruses.";
RL Nature 535:164-168(2016).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH JEV NS2B; WNV NS2B AND
RP ZIKV NS2B (MICROBIAL INFECTION).
RX PubMed=29593046; DOI=10.1128/jvi.00197-18;
RA Ma L., Li F., Zhang J.W., Li W., Zhao D.M., Wang H., Hua R.H., Bu Z.G.;
RT "Host Factor SPCS1 Regulates the Replication of Japanese Encephalitis Virus
RT through Interactions with Transmembrane Domains of NS2B.";
RL J. Virol. 92:0-0(2018).
RN [14] {ECO:0007744|PDB:7P2P, ECO:0007744|PDB:7P2Q}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.9 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE SIGNAL PEPTIDASE COMPLEX, AND PHOSPHORYLATION.
RX PubMed=34388369; DOI=10.1016/j.molcel.2021.07.031;
RA Liaci A.M., Steigenberger B., Telles de Souza P.C., Tamara S.,
RA Groellers-Mulderij M., Ogrissek P., Marrink S.J., Scheltema R.A.,
RA Foerster F.;
RT "Structure of the human signal peptidase complex reveals the determinants
RT for signal peptide cleavage.";
RL Mol. Cell 81:3934-3948.e11(2021).
CC -!- FUNCTION: Component of the signal peptidase complex (SPC) which
CC catalyzes the cleavage of N-terminal signal sequences from nascent
CC proteins as they are translocated into the lumen of the endoplasmic
CC reticulum (PubMed:34388369). Dispensable for SPC enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:P46965,
CC ECO:0000269|PubMed:34388369}.
CC -!- FUNCTION: (Microbial infection) Required for the post-translational
CC processing of proteins involved in virion assembly and secretion from
CC flaviviruses such as West Nile virus (WNV), Japanese encephalitis virus
CC (JEV), Dengue virus type 2 (DENV-2), Yellow Fever virus (YFV), Zika
CC virus (ZIKV) and hepatitis C virus (HCV) (PubMed:24009510,
CC PubMed:27383988, PubMed:29593046). Plays a key role in the post-
CC translational processing of flaviviral structural proteins prM, E, and
CC NS1 (PubMed:27383988, PubMed:29593046). In HCV, it is involved in
CC virion assembly where it promotes the interaction between HCV virus
CC proteins NS2 and E2 (PubMed:24009510). {ECO:0000269|PubMed:24009510,
CC ECO:0000269|PubMed:27383988, ECO:0000269|PubMed:29593046}.
CC -!- SUBUNIT: Component of the signal peptidase complex paralog A (SPC-A)
CC composed of a catalytic subunit SEC11A and three accessory subunits
CC SPCS1, SPCS2 and SPCS3 (PubMed:34388369). Component of the signal
CC peptidase complex paralog C (SPC-C) composed of a catalytic subunit
CC SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3
CC (PubMed:34388369). Within the complex, interacts with SPCS2 and SPCS3
CC (PubMed:34388369). The complex induces a local thinning of the ER
CC membrane which is used to measure the length of the signal peptide (SP)
CC h-region of protein substrates (PubMed:34388369). This ensures the
CC selectivity of the complex towards h-regions shorter than 18-20 amino
CC acids (PubMed:34388369). {ECO:0000269|PubMed:34388369}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus (HCV)
CC proteins NS2 and E2 (PubMed:24009510). Interacts with NS2B from
CC Japanese encephalitis virus (JEV), West Nile virus (WNV), and Zika
CC virus (ZIKV) (PubMed:29593046). {ECO:0000269|PubMed:24009510,
CC ECO:0000269|PubMed:29593046}.
CC -!- INTERACTION:
CC Q9Y6A9; PRO_0000045596 [Q99IB8]; Xeno; NbExp=4; IntAct=EBI-8852196, EBI-6901449;
CC Q9Y6A9; PRO_0000045598 [Q99IB8]; Xeno; NbExp=7; IntAct=EBI-8852196, EBI-6901421;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P83362}.
CC -!- PTM: May be phosphorylated. {ECO:0000269|PubMed:34388369}.
CC -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40380.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH00884.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL31361.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51320.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AC104446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65257.1; -; Genomic_DNA.
DR EMBL; AF092138; AAD40380.1; ALT_FRAME; mRNA.
DR EMBL; AK027426; BAG51320.1; ALT_INIT; mRNA.
DR EMBL; L38852; AAL31361.1; ALT_INIT; mRNA.
DR EMBL; BC000884; AAH00884.1; ALT_INIT; mRNA.
DR RefSeq; NP_054760.3; NM_014041.3.
DR PDB; 7P2P; EM; 4.90 A; D=1-169.
DR PDB; 7P2Q; EM; 4.90 A; D=1-169.
DR PDBsum; 7P2P; -.
DR PDBsum; 7P2Q; -.
DR AlphaFoldDB; Q9Y6A9; -.
DR SMR; Q9Y6A9; -.
DR BioGRID; 118796; 149.
DR ComplexPortal; CPX-2847; Signal peptidase complex, SEC11A variant.
DR ComplexPortal; CPX-7205; Signal peptidase complex, SEC11C variant.
DR IntAct; Q9Y6A9; 18.
DR MINT; Q9Y6A9; -.
DR STRING; 9606.ENSP00000478310; -.
DR GlyGen; Q9Y6A9; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; Q9Y6A9; -.
DR SwissPalm; Q9Y6A9; -.
DR BioMuta; SPCS1; -.
DR DMDM; 557952606; -.
DR EPD; Q9Y6A9; -.
DR jPOST; Q9Y6A9; -.
DR MassIVE; Q9Y6A9; -.
DR MaxQB; Q9Y6A9; -.
DR PaxDb; Q9Y6A9; -.
DR PeptideAtlas; Q9Y6A9; -.
DR PRIDE; Q9Y6A9; -.
DR ProteomicsDB; 86643; -.
DR TopDownProteomics; Q9Y6A9; -.
DR Antibodypedia; 46194; 86 antibodies from 19 providers.
DR DNASU; 28972; -.
DR Ensembl; ENST00000233025.11; ENSP00000233025.7; ENSG00000114902.14.
DR GeneID; 28972; -.
DR KEGG; hsa:28972; -.
DR UCSC; uc011bei.3; human.
DR UCSC; uc062kpj.1; human.
DR CTD; 28972; -.
DR DisGeNET; 28972; -.
DR GeneCards; SPCS1; -.
DR HGNC; HGNC:23401; SPCS1.
DR HPA; ENSG00000114902; Low tissue specificity.
DR MIM; 610358; gene.
DR neXtProt; NX_Q9Y6A9; -.
DR OpenTargets; ENSG00000114902; -.
DR PharmGKB; PA134972486; -.
DR VEuPathDB; HostDB:ENSG00000114902; -.
DR eggNOG; KOG4112; Eukaryota.
DR GeneTree; ENSGT00390000018321; -.
DR HOGENOM; CLU_134505_1_0_1; -.
DR InParanoid; Q9Y6A9; -.
DR OrthoDB; 1589808at2759; -.
DR PhylomeDB; Q9Y6A9; -.
DR TreeFam; TF106122; -.
DR PathwayCommons; Q9Y6A9; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR SignaLink; Q9Y6A9; -.
DR BioGRID-ORCS; 28972; 49 hits in 1080 CRISPR screens.
DR ChiTaRS; SPCS1; human.
DR GenomeRNAi; 28972; -.
DR Pharos; Q9Y6A9; Tbio.
DR PRO; PR:Q9Y6A9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6A9; protein.
DR Bgee; ENSG00000114902; Expressed in sperm and 204 other tissues.
DR ExpressionAtlas; Q9Y6A9; baseline and differential.
DR Genevisible; Q9Y6A9; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005787; C:signal peptidase complex; IPI:ComplexPortal.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; TAS:UniProtKB.
DR GO; GO:0006465; P:signal peptide processing; IDA:ComplexPortal.
DR GO; GO:0019082; P:viral protein processing; IMP:UniProtKB.
DR GO; GO:0019068; P:virion assembly; IMP:UniProtKB.
DR InterPro; IPR037713; Spc1.
DR InterPro; IPR009542; Spc1/SPCS1.
DR PANTHER; PTHR13202; PTHR13202; 1.
DR PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR Pfam; PF06645; SPC12; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..169
FT /note="Signal peptidase complex subunit 1"
FT /id="PRO_0000215154"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P83362"
FT REGION 91..169
FT /note="(Microbial infection) Interaction with JEV NS2B"
FT /evidence="ECO:0000269|PubMed:29593046"
FT REGION 110..169
FT /note="(Microbial infection) Interaction with HCV NS2 and
FT HCV E2"
FT /evidence="ECO:0000269|PubMed:24009510"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 41
FT /note="P -> A (in Ref. 6; AAH00884)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="I -> Y (in Ref. 5; AAL31361)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="L -> LAQ (in Ref. 6; AAH00884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 18298 MW; 65F180938A9BEF1E CRC64;
MARGGDTGCT GPSETSASGA AAIALPGLEG PATDAQCQTL PLTVLKSRSP SPRSLPPALS
CPPPQPAMLE HLSSLPTQMD YKGQKLAEQM FQGIILFSAI VGFIYGYVAE QFGWTVYIVM
AGFAFSCLLT LPPWPIYRRH PLKWLPVQES STDDKKPGER KIKRHAKNN
