SOGA1_HUMAN
ID SOGA1_HUMAN Reviewed; 1423 AA.
AC O94964; A6NK10; Q14DB2; Q5JW51; Q6ZTG8;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein SOGA1;
DE AltName: Full=SOGA family member 1;
DE AltName: Full=Suppressor of glucose by autophagy;
DE AltName: Full=Suppressor of glucose, autophagy-associated protein 1;
DE Contains:
DE RecName: Full=N-terminal form;
DE Contains:
DE RecName: Full=C-terminal 80 kDa form;
DE Short=80-kDa SOGA fragment;
GN Name=SOGA1; Synonyms=C20orf117, KIAA0889, SOGA;
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] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Cerebellum, and Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931 AND SER-1017, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20813965; DOI=10.2353/ajpath.2010.100363;
RA Cowerd R.B., Asmar M.M., Alderman J.M., Alderman E.A., Garland A.L.,
RA Busby W.H., Bodnar W.M., Rusyn I., Medoff B.D., Tisch R., Mayer-Davis E.,
RA Swenberg J.A., Zeisel S.H., Combs T.P.;
RT "Adiponectin lowers glucose production by increasing SOGA.";
RL Am. J. Pathol. 177:1936-1945(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Regulates autophagy by playing a role in the reduction of
CC glucose production in an adiponectin- and insulin-dependent manner.
CC {ECO:0000250}.
CC -!- SUBUNIT: The C-terminal 25 kDa form occurs as a monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC O94964-4; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-14083835, EBI-746752;
CC O94964-4; O14503: BHLHE40; NbExp=3; IntAct=EBI-14083835, EBI-711810;
CC O94964-4; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-14083835, EBI-2349927;
CC O94964-4; Q3B820: FAM161A; NbExp=3; IntAct=EBI-14083835, EBI-719941;
CC O94964-4; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-14083835, EBI-12094670;
CC O94964-4; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-14083835, EBI-1216080;
CC O94964-4; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-14083835, EBI-10172876;
CC O94964-4; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-14083835, EBI-1105153;
CC O94964-4; Q92753-1: RORB; NbExp=3; IntAct=EBI-14083835, EBI-18560266;
CC O94964-4; O75558: STX11; NbExp=3; IntAct=EBI-14083835, EBI-714135;
CC O94964-4; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-14083835, EBI-1105213;
CC O94964-4; Q99598: TSNAX; NbExp=3; IntAct=EBI-14083835, EBI-742638;
CC O94964-4; P17024: ZNF20; NbExp=3; IntAct=EBI-14083835, EBI-717634;
CC -!- SUBCELLULAR LOCATION: [C-terminal 80 kDa form]: Secreted {ECO:0000250}.
CC Note=Secreted in primary hepatocyte-conditioned media. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O94964-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94964-2; Sequence=VSP_035977;
CC Name=3;
CC IsoId=O94964-3; Sequence=VSP_035976, VSP_035978, VSP_035979;
CC Name=4;
CC IsoId=O94964-4; Sequence=VSP_040825, VSP_040826;
CC -!- INDUCTION: Up-regulated in the plasma by adiponectin in healthy fasting
CC female. {ECO:0000269|PubMed:20813965}.
CC -!- PTM: Proteolytically cleaved in primary hepatocytes into a C-terminal
CC 80 kDa form (By similarity). Proteolytically cleaved into a C-terminal
CC SOGA 25 kDa form that is detected in plasma. {ECO:0000250,
CC ECO:0000269|PubMed:20813965}.
CC -!- SIMILARITY: Belongs to the SOGA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74912.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020696; BAA74912.2; ALT_INIT; mRNA.
DR EMBL; AK022023; BAB13954.1; -; mRNA.
DR EMBL; AK126630; BAC86621.1; -; mRNA.
DR EMBL; AL079335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113405; AAI13406.1; -; mRNA.
DR EMBL; BC113433; AAI13434.1; -; mRNA.
DR CCDS; CCDS46598.1; -. [O94964-4]
DR CCDS; CCDS54459.1; -. [O94964-2]
DR RefSeq; NP_542194.2; NM_080627.3. [O94964-2]
DR RefSeq; NP_954650.2; NM_199181.2.
DR AlphaFoldDB; O94964; -.
DR SMR; O94964; -.
DR BioGRID; 126666; 107.
DR IntAct; O94964; 44.
DR MINT; O94964; -.
DR STRING; 9606.ENSP00000237536; -.
DR GlyGen; O94964; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94964; -.
DR PhosphoSitePlus; O94964; -.
DR BioMuta; SOGA1; -.
DR UCD-2DPAGE; O94964; -.
DR EPD; O94964; -.
DR jPOST; O94964; -.
DR MassIVE; O94964; -.
DR MaxQB; O94964; -.
DR PaxDb; O94964; -.
DR PeptideAtlas; O94964; -.
DR PRIDE; O94964; -.
DR ProteomicsDB; 50579; -. [O94964-1]
DR ProteomicsDB; 50580; -. [O94964-2]
DR ProteomicsDB; 50581; -. [O94964-3]
DR ProteomicsDB; 50582; -. [O94964-4]
DR Antibodypedia; 55174; 125 antibodies from 23 providers.
DR DNASU; 140710; -.
DR Ensembl; ENST00000237536.9; ENSP00000237536.4; ENSG00000149639.15. [O94964-2]
DR GeneID; 140710; -.
DR KEGG; hsa:140710; -.
DR MANE-Select; ENST00000237536.9; ENSP00000237536.4; NM_080627.4; NP_542194.2. [O94964-2]
DR UCSC; uc021wcx.2; human. [O94964-1]
DR CTD; 140710; -.
DR DisGeNET; 140710; -.
DR GeneCards; SOGA1; -.
DR HGNC; HGNC:16111; SOGA1.
DR HPA; ENSG00000149639; Tissue enriched (brain).
DR neXtProt; NX_O94964; -.
DR OpenTargets; ENSG00000149639; -.
DR PharmGKB; PA25657; -.
DR VEuPathDB; HostDB:ENSG00000149639; -.
DR eggNOG; KOG4787; Eukaryota.
DR GeneTree; ENSGT00950000182982; -.
DR HOGENOM; CLU_002595_0_0_1; -.
DR InParanoid; O94964; -.
DR OMA; HSDNKSC; -.
DR OrthoDB; 34629at2759; -.
DR PhylomeDB; O94964; -.
DR TreeFam; TF331853; -.
DR PathwayCommons; O94964; -.
DR SignaLink; O94964; -.
DR BioGRID-ORCS; 140710; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; SOGA1; human.
DR GeneWiki; C20orf117; -.
DR GenomeRNAi; 140710; -.
DR Pharos; O94964; Tbio.
DR PRO; PR:O94964; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O94964; protein.
DR Bgee; ENSG00000149639; Expressed in cerebellum and 165 other tissues.
DR ExpressionAtlas; O94964; baseline and differential.
DR Genevisible; O94964; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR InterPro; IPR027882; DUF4482.
DR InterPro; IPR027881; SOGA.
DR Pfam; PF14818; DUF4482; 1.
DR Pfam; PF11365; SOGA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..1423
FT /note="Protein SOGA1"
FT /id="PRO_0000050781"
FT CHAIN 1..688
FT /note="N-terminal form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000418054"
FT CHAIN 689..1421
FT /note="C-terminal 80 kDa form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000418055"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 688..689
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..871
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_035976"
FT VAR_SEQ 1
FT /note="M -> MEAPAAEPPVRGCGPQPAPAPAPAPERKKSHRAPSPARPKDVAGWSL
FT AKGRRGPGPGSAVACSAAFSSRPDKKGRAVAPGARGAGVRVAGVRTGVRAKGRPRSGAG
FT PRPPPPPPSLTDSSSEVSDCASEEARLLGLELALSSDAESAAGGPAGVRTGQPAQPAPS
FT AQQPPRPPASPDEPSVAASSVGSSRLPLSASLAFSDLTEEMLDCGPSGLVRELEELRSE
FT NDYLKDEIEELRAEM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035977"
FT VAR_SEQ 872..922
FT /note="RLSQLQKAADPWVLKHSELEKQDNSWKETRSEKIHDKEAVSEVELGGNGLK
FT -> MWDWAPTTSLQEVNKTVLVFALTQHTDQGGRPECALSVISTNNDVSSSVLR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_035978"
FT VAR_SEQ 1000..1016
FT /note="MQRSYTAPDKTGIRVYY -> KLPFLLILAPPQPPPIL (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040825"
FT VAR_SEQ 1017..1423
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040826"
FT VAR_SEQ 1374..1423
FT /note="DAVCDCSTQSLTSCFARSSRSAIRHSPSKCRLHPSESSWGGEERALPPSE
FT -> VGGWDLSFLLVGGVSI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_035979"
FT VARIANT 993
FT /note="Q -> H (in dbSNP:rs34459518)"
FT /id="VAR_056848"
SQ SEQUENCE 1423 AA; 159760 MW; EE50F4D144ABD972 CRC64;
MLEMRDVYME EDVYQLQELR QQLDQASKTC RILQYRLRKA ERRSLRAAQT GQVDGELIRG
LEQDVKVSKD ISMRLHKELE VVEKKRARLE EENEELRQRL IETELAKQVL QTELERPREH
SLKKRGTRSL GKADKKTLVQ EDSADLKCQL HFAKEESALM CKKLTKLAKE NDSMKEELLK
YRSLYGDLDS ALSAEELADA PHSRETELKV HLKLVEEEAN LLSRRIVELE VENRGLRAEM
DDMKDHGGGC GGPEARLAFS ALGGGECGES LAELRRHLQF VEEEAELLRR SSAELEDQNK
LLLNELAKFR SEHELDVALS EDSCSVLSEP SQEELAAAKL QIGELSGKVK KLQYENRVLL
SNLQRCDLAS CQSTRPMLET DAEAGDSAQC VPAPLGETHE SHAVRLCRAR EAEVLPGLRE
QAALVSKAID VLVADANGFT AGLRLCLDNE CADFRLHEAP DNSEGPRDTK LIHAILVRLS
VLQQELNAFT RKADAVLGCS VKEQQESFSS LPPLGSQGLS KEILLAKDLG SDFQPPDFRD
LPEWEPRIRE AFRTGDLDSK PDPSRSFRPY RAEDNDSYAS EIKELQLVLA EAHDSLRGLQ
EQLSQERQLR KEEADNFNQK MVQLKEDQQR ALLRREFELQ SLSLQRRLEQ KFWSQEKNML
VQESQQFKHN FLLLFMKLRW FLKRWRQGKV LPSEGDDFLE VNSMKELYLL MEEEEINAQH
SDNKACTGDS WTQNTPNEYI KTLADMKVTL KELCWLLRDE RRGLTELQQQ FAKAKATWET
ERAELKGHTS QMELKTGKGA GERAGPDWKA ALQREREEQQ HLLAESYSAV MELTRQLQIS
ERNWSQEKLQ LVERLQGEKQ QVEQQVKELQ NRLSQLQKAA DPWVLKHSEL EKQDNSWKET
RSEKIHDKEA VSEVELGGNG LKRTKSVSSM SEFESLLDCS PYLAGGDARG KKLPNNPAFG
FVSSEPGDPE KDTKEKPGLS SRDCNHLGAL ACQDPPGRQM QRSYTAPDKT GIRVYYSPPV
ARRLGVPVVH DKEGKIIIEP GFLFTTAKPK ESAEADGLAE SSYGRWLCNF SRQRLDGGSA
GSPSAAGPGF PAALHDFEMS GNMSDDMKEI TNCVRQAMRS GSLERKVKST SSQTVGLASV
GTQTIRTVSV GLQTDPPRSS LHGKAWSPRS SSLVSVRSKQ ISSSLDKVHS RIERPCCSPK
YGSPKLQRRS VSKLDSSKDR SLWNLHQGKQ NGSAWARSTT TRDSPVLRNI NDGLSSLFSV
VEHSGSTESV WKLGMSETRA KPEPPKYGIV QEFFRNVCGR APSPTSSAGE EGTKKPEPLS
PASYHQPEGV ARILNKKAAK LGSSEEVRLT MLPQVGKDGV LRDGDGAVVL PNEDAVCDCS
TQSLTSCFAR SSRSAIRHSP SKCRLHPSES SWGGEERALP PSE
