SEMG1_HUMAN
ID SEMG1_HUMAN Reviewed; 462 AA.
AC P04279; Q53ZV0; Q53ZV1; Q53ZV2; Q6X4I9; Q6Y809; Q6Y822; Q6Y823; Q86U64;
AC Q96QM3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Semenogelin-1;
DE AltName: Full=Cancer/testis antigen 103;
DE AltName: Full=Semenogelin I;
DE Short=SGI;
DE Contains:
DE RecName: Full=Alpha-inhibin-92;
DE Contains:
DE RecName: Full=Alpha-inhibin-31;
DE Contains:
DE RecName: Full=Seminal basic protein;
DE Flags: Precursor;
GN Name=SEMG1; Synonyms=SEMG;
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), AND PYROGLUTAMATE FORMATION AT
RP GLN-24.
RX PubMed=2912989; DOI=10.1016/s0021-9258(18)94272-9;
RA Lilja H., Abrahamsson P.-A., Lundwall A.;
RT "Semenogelin, the predominant protein in human semen. Primary structure and
RT identification of closely related proteins in the male accessory sex glands
RT and on the spermatozoa.";
RL J. Biol. Chem. 264:1894-1900(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1517240; DOI=10.1016/s0021-9258(19)37155-8;
RA Ulvsbaeck M., Lazure C., Lilja H., Spurr N.K., Rao V.V., Loeffler C.,
RA Hansmann I., Lundwall A.;
RT "Gene structure of semenogelin I and II. The predominant proteins in human
RT semen are encoded by two homologous genes on chromosome 20.";
RL J. Biol. Chem. 267:18080-18084(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-79 AND LEU-372.
RX PubMed=14629036; DOI=10.1007/s00239-003-2474-x;
RA Jensen-Seaman M.I., Li W.-H.;
RT "Evolution of the hominoid semenogelin genes, the major proteins of
RT ejaculated semen.";
RL J. Mol. Evol. 57:261-270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-237 AND 241-449, AND VARIANT
RP THR-79.
RX PubMed=14562960; DOI=10.1007/s00239-002-2463-0;
RA Kingan S.B., Tatar M., Rand D.M.;
RT "Reduced polymorphism in the chimpanzee semen coagulating protein,
RT semenogelin I.";
RL J. Mol. Evol. 57:159-169(2003).
RN [9]
RP PROTEIN SEQUENCE OF 108-159.
RX PubMed=3972122; DOI=10.1016/0014-5793(85)81179-0;
RA Lilja H., Jeppsson J.-O.;
RT "Amino acid sequence of the predominant basic protein in human seminal
RT plasma.";
RL FEBS Lett. 182:181-184(1985).
RN [10]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6698208; DOI=10.1016/0014-5793(84)80840-6;
RA Seidah N.G., Ramasharma K., Sairam M.R., Chretien M.;
RT "Partial amino acid sequence of a human seminal plasma peptide with
RT inhibin-like activity.";
RL FEBS Lett. 167:98-102(1984).
RN [11]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6422553; DOI=10.1126/science.6422553;
RA Ramasharma K., Sairam M.R., Seidah N.G., Chretien M., Manjunath P.,
RA Schiller P.W., Yamashiro D., Li C.H.;
RT "Isolation, structure, and synthesis of a human seminal plasma peptide with
RT inhibin-like activity.";
RL Science 223:1199-1202(1984).
RN [12]
RP PROTEIN SEQUENCE OF 316-344.
RX PubMed=2757795;
RA Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.;
RT "Isolation and structure determination of two peptides occurring in human
RT seminal plasma.";
RL Biol. Chem. Hoppe-Seyler 370:353-356(1989).
RN [13]
RP PROTEIN SEQUENCE OF 373-397.
RX PubMed=8444163; DOI=10.1111/j.1432-1033.1993.tb17629.x;
RA Khan Z., Smyth D.G.;
RT "Isolation and identification of N-terminally extended forms of 5-
RT oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-releasing-
RT hormone (TRH)-like peptide present in human semen.";
RL Eur. J. Biochem. 212:35-40(1993).
RN [14]
RP PROTEIN SEQUENCE OF 68-159.
RX PubMed=3889920; DOI=10.1073/pnas.82.12.4041;
RA Li C.H., Hammonds R.G., Ramasharma K., Chung D.;
RT "Human seminal alpha inhibins: isolation, characterization, and
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4041-4044(1985).
RN [15]
RP REVIEW.
RX PubMed=10412373; DOI=10.1007/s000180050346;
RA Robert M., Gagnon C.;
RT "Semenogelin I: a coagulum forming, multifunctional seminal vesicle
RT protein.";
RL Cell. Mol. Life Sci. 55:944-960(1999).
RN [16]
RP INTERACTION WITH EPPIN.
RX PubMed=15590901; DOI=10.1095/biolreprod.104.036483;
RA Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.;
RT "Association of eppin with semenogelin on human spermatozoa.";
RL Biol. Reprod. 72:1064-1070(2005).
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH LTF; CLU AND EPPIN.
RX PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
RA Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
RT "Characterization of an eppin protein complex from human semen and
RT spermatozoa.";
RL Biol. Reprod. 77:476-484(2007).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF CYS-239.
RX PubMed=19889947; DOI=10.1095/biolreprod.109.081331;
RA Mitra A., Richardson R.T., O'Rand M.G.;
RT "Analysis of recombinant human semenogelin as an inhibitor of human sperm
RT motility.";
RL Biol. Reprod. 82:489-496(2010).
CC -!- FUNCTION: Predominant protein in semen. It participates in the
CC formation of a gel matrix entrapping the accessory gland secretions and
CC ejaculated spermatozoa. Fragments of semenogelin and/or fragments of
CC the related proteins may contribute to the activation of progressive
CC sperm movements as the gel-forming proteins are fragmented by KLK3/PSA.
CC {ECO:0000269|PubMed:19889947}.
CC -!- FUNCTION: Alpha-inhibin-92 and alpha-inhibin-31, derived from the
CC proteolytic degradation of semenogelin, inhibit the secretion of
CC pituitary follicle-stimulating hormone. {ECO:0000269|PubMed:19889947}.
CC -!- SUBUNIT: Occurs in disulfide-linked complexes which may also contain
CC two less abundant 71- and 76-kDa semenogelin-related polypeptides.
CC Interacts with EPPIN (via C-terminus); Cys-239 is a critical amino acid
CC for both binding to EPPIN. {ECO:0000269|PubMed:15590901,
CC ECO:0000269|PubMed:17567961}.
CC -!- INTERACTION:
CC P04279-2; Q96JC9: EAF1; NbExp=3; IntAct=EBI-12272118, EBI-769261;
CC P04279-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12272118, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04279-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04279-2; Sequence=VSP_004385;
CC -!- TISSUE SPECIFICITY: Seminal vesicle.
CC -!- PTM: Transglutaminase substrate.
CC -!- PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in
CC liquefaction of the semen coagulum and the progressive release of
CC motile spermatozoa.
CC -!- SIMILARITY: Belongs to the semenogelin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shackled sperm - Issue 62 of
CC September 2005;
CC URL="https://web.expasy.org/spotlight/back_issues/062";
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; J04440; AAB59506.1; -; mRNA.
DR EMBL; Z47556; CAA87636.1; -; Genomic_DNA.
DR EMBL; M81650; AAA18168.1; -; Genomic_DNA.
DR EMBL; AY256465; AAP82462.1; -; Genomic_DNA.
DR EMBL; AY256466; AAP82463.1; -; Genomic_DNA.
DR EMBL; AY256467; AAP82464.1; -; Genomic_DNA.
DR EMBL; AY256468; AAP82465.1; -; Genomic_DNA.
DR EMBL; AY256469; AAP82466.1; -; Genomic_DNA.
DR EMBL; BT007177; AAP35841.1; -; mRNA.
DR EMBL; AL049767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75871.1; -; Genomic_DNA.
DR EMBL; BC007096; AAH07096.1; -; mRNA.
DR EMBL; BC055416; AAH55416.1; -; mRNA.
DR EMBL; AY174423; AAO20112.1; -; Genomic_DNA.
DR EMBL; AY174424; AAO20113.1; -; Genomic_DNA.
DR EMBL; AY174437; AAO20126.1; -; Genomic_DNA.
DR CCDS; CCDS13345.1; -. [P04279-1]
DR PIR; B43412; WTHUB.
DR RefSeq; NP_002998.1; NM_003007.4. [P04279-1]
DR AlphaFoldDB; P04279; -.
DR BioGRID; 112306; 102.
DR IntAct; P04279; 30.
DR MINT; P04279; -.
DR STRING; 9606.ENSP00000361867; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR iPTMnet; P04279; -.
DR PhosphoSitePlus; P04279; -.
DR BioMuta; SEMG1; -.
DR DMDM; 134426; -.
DR jPOST; P04279; -.
DR MassIVE; P04279; -.
DR MaxQB; P04279; -.
DR PaxDb; P04279; -.
DR PeptideAtlas; P04279; -.
DR PRIDE; P04279; -.
DR ProteomicsDB; 51699; -. [P04279-1]
DR ProteomicsDB; 51700; -. [P04279-2]
DR Antibodypedia; 12686; 237 antibodies from 29 providers.
DR DNASU; 6406; -.
DR Ensembl; ENST00000372781.4; ENSP00000361867.3; ENSG00000124233.12. [P04279-1]
DR GeneID; 6406; -.
DR KEGG; hsa:6406; -.
DR MANE-Select; ENST00000372781.4; ENSP00000361867.3; NM_003007.5; NP_002998.1.
DR UCSC; uc002xni.3; human. [P04279-1]
DR CTD; 6406; -.
DR DisGeNET; 6406; -.
DR GeneCards; SEMG1; -.
DR HGNC; HGNC:10742; SEMG1.
DR HPA; ENSG00000124233; Tissue enriched (seminal).
DR MIM; 182140; gene.
DR neXtProt; NX_P04279; -.
DR OpenTargets; ENSG00000124233; -.
DR PharmGKB; PA35664; -.
DR VEuPathDB; HostDB:ENSG00000124233; -.
DR eggNOG; ENOG502T80H; Eukaryota.
DR GeneTree; ENSGT00940000162560; -.
DR HOGENOM; CLU_034710_0_0_1; -.
DR InParanoid; P04279; -.
DR OMA; HEQKVRH; -.
DR OrthoDB; 305064at2759; -.
DR PhylomeDB; P04279; -.
DR TreeFam; TF342360; -.
DR PathwayCommons; P04279; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P04279; -.
DR BioGRID-ORCS; 6406; 11 hits in 1057 CRISPR screens.
DR ChiTaRS; SEMG1; human.
DR GeneWiki; Semenogelin_I; -.
DR GenomeRNAi; 6406; -.
DR Pharos; P04279; Tbio.
DR PRO; PR:P04279; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P04279; protein.
DR Bgee; ENSG00000124233; Expressed in seminal vesicle and 65 other tissues.
DR Genevisible; P04279; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0050817; P:coagulation; IDA:UniProtKB.
DR GO; GO:0007320; P:insemination; TAS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0090281; P:negative regulation of calcium ion import; IDA:CACAO.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; IDA:CACAO.
DR GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR InterPro; IPR008836; Semenogelin.
DR Pfam; PF05474; Semenogelin; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..462
FT /note="Semenogelin-1"
FT /id="PRO_0000032351"
FT PEPTIDE 68..159
FT /note="Alpha-inhibin-92"
FT /id="PRO_0000032352"
FT PEPTIDE 108..159
FT /note="Seminal basic protein"
FT /id="PRO_0000032353"
FT PEPTIDE 108..138
FT /note="Alpha-inhibin-31"
FT /id="PRO_0000032354"
FT REPEAT 70..129
FT /note="3-1"
FT REPEAT 141..200
FT /note="2-1"
FT REPEAT 201..260
FT /note="2-2"
FT REPEAT 381..439
FT /note="3-2"
FT REGION 24..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..439
FT /note="Repeat-rich region"
FT /evidence="ECO:0000250"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..283
FT /note="Interaction with EPPIN"
FT /evidence="ECO:0000269|PubMed:15590901"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..380
FT /note="2 X 60 AA tandem repeats, type 1"
FT REGION 270..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:2912989"
FT DISULFID 239
FT /note="Interchain"
FT VAR_SEQ 312..371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_004385"
FT VARIANT 58
FT /note="E -> G (in dbSNP:rs11559137)"
FT /id="VAR_053650"
FT VARIANT 79
FT /note="S -> T (less common genetic variant;
FT dbSNP:rs2301366)"
FT /evidence="ECO:0000269|PubMed:14562960,
FT ECO:0000269|PubMed:14629036"
FT /id="VAR_005610"
FT VARIANT 108
FT /note="H -> R (in dbSNP:rs2233884)"
FT /id="VAR_053651"
FT VARIANT 372
FT /note="R -> L (in dbSNP:rs2233887)"
FT /evidence="ECO:0000269|PubMed:14629036"
FT /id="VAR_022679"
FT MUTAGEN 239
FT /note="C->G: Abrogates binding to EPPIN and do not inhibit
FT spem motility."
FT /evidence="ECO:0000269|PubMed:19889947"
FT CONFLICT 100
FT /note="L -> Q (in Ref. 3; AAP82463)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..237
FT /note="QTS -> LRT (in Ref. 8; AAO20112/AAO20113)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="K -> L (in Ref. 12; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="K -> N (in Ref. 2; CAA87636/AAA18168)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="R -> Q (in Ref. 4 and 7)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52131 MW; 760F48EFCF2FA702 CRC64;
MKPNIIFVLS LLLILEKQAA VMGQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK
GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK
GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG
AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP
AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY
GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY
GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH
EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT
