ID   GAG_HV1A2               Reviewed;         502 AA.
AC   P03349;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 175.
DE   RecName: Full=Gag polyprotein;
DE   AltName: Full=Pr55Gag;
DE   Contains:
DE     RecName: Full=Matrix protein p17;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=Capsid protein p24;
DE              Short=CA;
DE   Contains:
DE     RecName: Full=Spacer peptide 1 {ECO:0000250|UniProtKB:P12493};
DE              Short=SP1;
DE     AltName: Full=p2;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p7;
DE              Short=NC;
DE   Contains:
DE     RecName: Full=Spacer peptide 2 {ECO:0000250|UniProtKB:P12493};
DE              Short=SP2;
DE     AltName: Full=p1;
DE   Contains:
DE     RecName: Full=p6-gag;
GN   Name=gag;
OS   Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
OS   (HIV-1).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Lentivirus humimdef1; Human immunodeficiency virus type 1.
OX   NCBI_TaxID=11685;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2578227; DOI=10.1126/science.2578227;
RA   Sanchez-Pescador R., Power M.D., Barr P.J., Steimer K.S., Stempien M.M.,
RA   Brown-Shimer S.L., Gee W.W., Renard A., Randolph A., Levy J.A., Dina D.,
RA   Luciw P.A.;
RT   "Nucleotide sequence and expression of an AIDS-associated retrovirus (ARV-
RT   2).";
RL   Science 227:484-492(1985).
RN   [2]
RP   REVIEW.
RX   PubMed=12873766; DOI=10.1016/s0005-2736(03)00163-9;
RA   Scarlata S., Carter C.;
RT   "Role of HIV-1 Gag domains in viral assembly.";
RL   Biochim. Biophys. Acta 1614:62-72(2003).
RN   [3]
RP   INTERACTION WITH HOST PACSIN2, AND MUTAGENESIS OF THR-458; LEU-491; LEU-494
RP   AND PHE-495.
RX   PubMed=29891700; DOI=10.1073/pnas.1801849115;
RA   Popov S., Popova E., Inoue M., Wu Y., Goettlinger H.;
RT   "HIV-1 gag recruits PACSIN2 to promote virus spreading.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:7093-7098(2018).
CC   -!- FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the
CC       essential events in virion assembly, including binding the plasma
CC       membrane, making the protein-protein interactions necessary to create
CC       spherical particles, recruiting the viral Env proteins, and packaging
CC       the genomic RNA via direct interactions with the RNA packaging sequence
CC       (Psi). {ECO:0000250|UniProtKB:P04591}.
CC   -!- FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma
CC       membrane via a multipartite membrane-binding signal, that includes its
CC       myristoylated N-terminus (By similarity). Matrix protein is part of the
CC       pre-integration complex. Implicated in the release from host cell
CC       mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P12493}.
CC   -!- FUNCTION: [Capsid protein p24]: Forms the conical core that
CC       encapsulates the genomic RNA-nucleocapsid complex in the virion. Most
CC       core are conical, with only 7% tubular. The core is constituted by
CC       capsid protein hexamer subunits. The core is disassembled soon after
CC       virion entry (By similarity). The capsid promotes immune invasion by
CC       cloaking viral DNA from CGAS detection (By similarity). Host
CC       restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral
CC       capsids and cause premature capsid disassembly, leading to blocks in
CC       reverse transcription. Capsid restriction by TRIM5 is one of the
CC       factors which restricts HIV-1 to the human species. Host PIN1
CC       apparently facilitates the virion uncoating (By similarity). On the
CC       other hand, interactions with PDZD8 or CYPA stabilize the capsid (By
CC       similarity). {ECO:0000250|UniProtKB:P04591,
CC       ECO:0000250|UniProtKB:P12493}.
CC   -!- FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral
CC       dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC       fingers. Acts as a nucleic acid chaperone which is involved in
CC       rearangement of nucleic acid secondary structure during gRNA
CC       retrotranscription. Also facilitates template switch leading to
CC       recombination. As part of the polyprotein, participates in gRNA
CC       dimerization, packaging, tRNA incorporation and virion assembly.
CC       {ECO:0000250|UniProtKB:P04591}.
CC   -!- FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle
CC       by interacting with the host class E VPS proteins TSG101 and
CC       PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBUNIT: [Gag polyprotein]: Homotrimer; further assembles as hexamers
CC       of trimers (By similarity). Oligomerization possibly creates a central
CC       hole into which the cytoplasmic tail of the gp41 envelope protein may
CC       be inserted. Interacts with host TRIM22; this interaction seems to
CC       disrupt proper trafficking of Gag polyprotein and may interfere with
CC       budding (By similarity). Interacts with host PDZD8 (By similarity).
CC       When ubiquitinated, interacts (via p6-gag domain) with host PACSIN2;
CC       this interaction allows PACSIN2 recruitment to viral assembly sites and
CC       its subsequent incorporation into virions (PubMed:29891700). Interacts
CC       with MOV10 (By similarity). {ECO:0000250|UniProtKB:P04591,
CC       ECO:0000269|PubMed:29891700}.
CC   -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC       hexamers of trimers. Interacts with gp41 (via C-terminus). Interacts
CC       with host CALM1; this interaction induces a conformational change in
CC       the Matrix protein, triggering exposure of the myristate group.
CC       Interacts with host AP3D1; this interaction allows the polyprotein
CC       trafficking to multivesicular bodies during virus assembly. Part of the
CC       pre-integration complex (PIC) which is composed of viral genome, matrix
CC       protein, Vpr and integrase. {ECO:0000250|UniProtKB:P04591,
CC       ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC       multimerizes as homohexamers or homopentamers (By similarity).
CC       Interacts with host NUP98 (By similarity). Interacts with host
CC       PPIA/CYPA; this interaction stabilizes the capsid (By similarity).
CC       Interacts with host NUP153 (By similarity). Interacts with host PDZD8;
CC       this interaction stabilizes the capsid. Interacts with host TRIM5; this
CC       interaction destabilizes the capsid (By similarity). Interacts with
CC       host CPSF6 (By similarity). Interacts with host NONO; the interaction
CC       is weak (By similarity). {ECO:0000250|UniProtKB:P04591,
CC       ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBUNIT: [Nucleocapsid protein p7]: Interacts with host NUP98.
CC       {ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBUNIT: [p6-gag]: Interacts with Vpr; this interaction allows Vpr
CC       incorporation into the virion (By similarity). Interacts with host
CC       TSG101 (By similarity). Interacts with host PDCD6IP/AIP1 (By
CC       similarity). {ECO:0000250|UniProtKB:P03348,
CC       ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane
CC       {ECO:0000250|UniProtKB:P12493}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body
CC       {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably
CC       linked to virus assembly sites. The main location is the cell membrane,
CC       but under some circumstances, late endosomal compartments can serve as
CC       productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane
CC       {ECO:0000250|UniProtKB:P12493}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host
CC       cytoplasm {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC       {ECO:0000250|UniProtKB:P12493}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion
CC       {ECO:0000250|UniProtKB:P12493}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC         Comment=Translation results in the formation of the Gag polyprotein
CC         most of the time. Ribosomal frameshifting at the gag-pol genes
CC         boundary occurs at low frequency and produces the Gag-Pol
CC         polyprotein. This strategy of translation probably allows the virus
CC         to modulate the quantity of each viral protein. Maintenance of a
CC         correct Gag to Gag-Pol ratio is essential for RNA dimerization and
CC         viral infectivity.;
CC       Name=Gag polyprotein;
CC         IsoId=P03349-1; Sequence=Displayed;
CC       Name=Gag-Pol polyprotein;
CC         IsoId=P03369-1; Sequence=External;
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle budding. They recruit proteins of the host
CC       ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC       ESCRT-associated proteins. p6-gag contains two L domains: a PTAP/PSAP
CC       motif, which interacts with the UEV domain of TSG101 and a LYPX(n)L
CC       motif which interacts with PDCD6IP/AIP1.
CC       {ECO:0000250|UniProtKB:P12493}.
CC   -!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral
CC       protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.
CC   -!- PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the
CC       virion by a host kinase. Phosphorylation is apparently not a major
CC       regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.
CC   -!- PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this
CC       phosphorylation is necessary for Pin1-mediated virion uncoating.
CC       {ECO:0000250|UniProtKB:P12493}.
CC   -!- PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its
CC       function by reducing RNA annealing and the initiation of reverse
CC       transcription. {ECO:0000250|UniProtKB:P03347}.
CC   -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC       Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC       majority of strains found worldwide belong to the group M. Group O
CC       seems to be endemic to and largely confined to Cameroon and neighboring
CC       countries in West Central Africa, where these viruses represent a small
CC       minority of HIV-1 strains. The group N is represented by a limited
CC       number of isolates from Cameroonian persons. The group M is further
CC       subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC   -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC       translation.
CC   -!- SIMILARITY: Belongs to the primate lentivirus group gag polyprotein
CC       family. {ECO:0000305}.
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DR   EMBL; K02007; AAB59875.1; -; Genomic_RNA.
DR   PIR; A03947; FOVWA2.
DR   PDB; 4OBD; X-ray; 1.90 A; E/F=446-455.
DR   PDB; 4OBF; X-ray; 1.68 A; E/F=446-455.
DR   PDB; 4OBG; X-ray; 1.78 A; E/F=446-455.
DR   PDB; 4OBH; X-ray; 1.85 A; E/F=446-455.
DR   PDB; 4OBJ; X-ray; 1.75 A; C=446-455.
DR   PDB; 4OBK; X-ray; 1.65 A; C=446-455.
DR   PDB; 4QJ2; X-ray; 2.13 A; F/G=446-455.
DR   PDB; 4QJ6; X-ray; 1.50 A; E/F=446-455.
DR   PDB; 4QJ7; X-ray; 1.67 A; F/G=446-455.
DR   PDB; 4QJ8; X-ray; 2.00 A; E/F=446-454.
DR   PDB; 4QJ9; X-ray; 1.83 A; G=446-455.
DR   PDB; 4QJA; X-ray; 1.54 A; P=446-454.
DR   BMRB; P03349; -.
DR   SMR; P03349; -.
DR   EvolutionaryTrace; P03349; -.
DR   PRO; PR:P03349; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
DR   GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
DR   FunFam; 1.10.1200.30:FF:000001; Gag polyprotein; 1.
DR   FunFam; 1.10.150.90:FF:000001; Gag polyprotein; 1.
DR   FunFam; 1.10.375.10:FF:000001; Gag polyprotein; 1.
DR   FunFam; 1.20.5.760:FF:000001; Gag polyprotein; 1.
DR   FunFam; 4.10.60.10:FF:000001; Gag polyprotein; 1.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 6.10.250.390; -; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 1.10.150.90; Immunodeficiency lentiviruses, gag gene matrix protein p17; 1.
DR   Gene3D; 1.20.5.760; Single helix bin; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR045345; Gag_p24_C.
DR   InterPro; IPR014817; Gag_p6.
DR   InterPro; IPR000071; Lentvrl_matrix_N.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR050195; Primate_lentivir_Gag_pol-like.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR40389:SF4; -; 1.
DR   PANTHER; PTHR40389; ENDOGENOUS RETROVIRUS GROUP K MEMBER 24 GAG POLYPROTEIN-RELATED; 1.
DR   Pfam; PF00540; Gag_p17; 1.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF08705; Gag_p6; 1.
DR   Pfam; PF00098; zf-CCHC; 2.
DR   PRINTS; PR00234; HIV1MATRIX.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
DR   PDBsum; 4OBD; -.
DR   PDBsum; 4OBF; -.
DR   PDBsum; 4OBG; -.
DR   PDBsum; 4OBH; -.
DR   PDBsum; 4OBJ; -.
DR   PDBsum; 4OBK; -.
DR   PDBsum; 4QJ2; -.
DR   PDBsum; 4QJ6; -.
DR   PDBsum; 4QJ7; -.
DR   PDBsum; 4QJ8; -.
DR   PDBsum; 4QJ9; -.
DR   PDBsum; 4QJA; -.
PE   1: Evidence at protein level;
KW   3D-structure; AIDS; Capsid protein; Host cell membrane; Host cytoplasm;
KW   Host endosome; Host membrane; Host nucleus; Host-virus interaction;
KW   Lipoprotein; Membrane; Metal-binding; Methylation; Myristate;
KW   Phosphoprotein; Repeat; Ribosomal frameshifting; RNA-binding;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..502
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000261208"
FT   CHAIN           2..134
FT                   /note="Matrix protein p17"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038505"
FT   CHAIN           135..365
FT                   /note="Capsid protein p24"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038506"
FT   PEPTIDE         366..379
FT                   /note="Spacer peptide 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038507"
FT   CHAIN           380..434
FT                   /note="Nucleocapsid protein p7"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038508"
FT   PEPTIDE         435..450
FT                   /note="Spacer peptide 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038509"
FT   CHAIN           451..502
FT                   /note="p6-gag"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038510"
FT   ZN_FING         392..409
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         413..430
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          7..31
FT                   /note="Interaction with Gp41"
FT                   /evidence="ECO:0000250|UniProtKB:P12493"
FT   REGION          8..43
FT                   /note="Interaction with host CALM1"
FT                   /evidence="ECO:0000250|UniProtKB:P04591"
FT   REGION          12..19
FT                   /note="Interaction with host AP3D1"
FT                   /evidence="ECO:0000250|UniProtKB:P12497"
FT   REGION          14..33
FT                   /note="Interaction with membrane phosphatidylinositol 4,5-
FT                   bisphosphate and RNA"
FT                   /evidence="ECO:0000250|UniProtKB:P12493"
FT   REGION          73..77
FT                   /note="Interaction with membrane phosphatidylinositol 4,5-
FT                   bisphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P12493"
FT   REGION          106..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..229
FT                   /note="Interaction with host PPIA/CYPA and NUP153"
FT                   /evidence="ECO:0000250|UniProtKB:P12493"
FT   REGION          219..227
FT                   /note="PPIA/CYPA-binding loop"
FT                   /evidence="ECO:0000250|UniProtKB:P04591"
FT   REGION          279..365
FT                   /note="Dimerization/Multimerization of capsid protein p24"
FT                   /evidence="ECO:0000250|UniProtKB:P04591"
FT   REGION          446..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           16..22
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           26..32
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           457..460
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           485..494
FT                   /note="LYPX(n)L motif"
FT   COMPBIAS        463..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            134..135
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            365..366
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            379..380
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            434..435
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            450..451
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         150
FT                   /note="Phosphoserine; by host MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P12493"
FT   MOD_RES         389
FT                   /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT                   p7; by host PRMT6"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         411
FT                   /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT                   p7; by host PRMT6"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         458
FT                   /note="T->G: No effect on host PACSIN2 incorporation into
FT                   virions."
FT                   /evidence="ECO:0000269|PubMed:29891700"
FT   MUTAGEN         491
FT                   /note="L->A: No effect on host PACSIN2 incorporation into
FT                   virions."
FT                   /evidence="ECO:0000269|PubMed:29891700"
FT   MUTAGEN         494
FT                   /note="L->P: Slight decrease in host PACSIN2 incorporation
FT                   into virions."
FT                   /evidence="ECO:0000269|PubMed:29891700"
FT   MUTAGEN         495
FT                   /note="F->S: Slight decrease in host PACSIN2 incorporation
FT                   into virions."
FT                   /evidence="ECO:0000269|PubMed:29891700"
SQ   SEQUENCE   502 AA;  56066 MW;  EF36C928D5F816E7 CRC64;
     MGARASVLSG GELDKWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
     LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIDVKDTKEA LEKIEEEQNK SKKKAQQAAA
     AAGTGNSSQV SQNYPIVQNL QGQMVHQAIS PRTLNAWVKV VEEKAFSPEV IPMFSALSEG
     ATPQDLNTML NTVGGHQAAM QMLKETINEE AAEWDRVHPV HAGPIAPGQM REPRGSDIAG
     TTSTLQEQIG WMTNNPPIPV GEIYKRWIIL GLNKIVRMYS PTSILDIRQG PKEPFRDYVD
     RFYKTLRAEQ ASQDVKNWMT ETLLVQNANP DCKTILKALG PAATLEEMMT ACQGVGGPGH
     KARVLAEAMS QVTNPANIMM QRGNFRNQRK TVKCFNCGKE GHIAKNCRAP RKKGCWRCGR
     EGHQMKDCTE RQANFLGKIW PSYKGRPGNF LQSRPEPTAP PEESFRFGEE KTTPSQKQEP
     IDKELYPLTS LRSLFGNDPS SQ
//