UNC84_CAEEL
ID UNC84_CAEEL Reviewed; 1111 AA.
AC Q20745; Q9U475; Q9U476;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nuclear migration and anchoring protein unc-84;
DE AltName: Full=Uncoordinated protein 84;
GN Name=unc-84 {ECO:0000312|WormBase:F54B11.3a};
GN ORFNames=F54B11.3 {ECO:0000312|WormBase:F54B11.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 1-MET--ARG-208;
RP 40-LEU--LYS-161; PRO-91; ASP-932; ARG-984; SER-988; CYS-994 AND GLY-1002.
RC STRAIN=Bristol N2; TISSUE=Embryo;
RX PubMed=10375507; DOI=10.1242/dev.126.14.3171;
RA Malone C.J., Fixsen W.D., Horvitz H.R., Han M.;
RT "UNC-84 localizes to the nuclear envelope and is required for nuclear
RT migration and anchoring during C. elegans development.";
RL Development 126:3171-3181(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, INTERACTION WITH UNC-83, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1-MET--ARG-208; PRO-91; ASP-932; ARG-984; SER-988 AND GLY-1002.
RX PubMed=11748140; DOI=10.1242/dev.128.24.5039;
RA Starr D.A., Hermann G.J., Malone C.J., Fixsen W., Priess J.R.,
RA Horvitz H.R., Han M.;
RT "unc-83 encodes a novel component of the nuclear envelope and is essential
RT for proper nuclear migration.";
RL Development 128:5039-5050(2001).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11870211; DOI=10.1242/jcs.115.5.923;
RA Gruenbaum Y., Lee K.K., Liu J., Cohen M., Wilson K.L.;
RT "The expression, lamin-dependent localization and RNAi depletion phenotype
RT for emerin in C. elegans.";
RL J. Cell Sci. 115:923-929(2002).
RN [5]
RP FUNCTION, INTERACTION WITH ANC-1, AND MUTAGENESIS OF PRO-91 AND GLY-1002.
RX PubMed=12169658; DOI=10.1126/science.1075119;
RA Starr D.A., Han M.;
RT "Role of ANC-1 in tethering nuclei to the actin cytoskeleton.";
RL Science 298:406-409(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF ASP-932; ARG-984; SER-988 AND GLY-1002.
RX PubMed=11907270; DOI=10.1091/mbc.01-06-0294;
RA Lee K.K., Starr D.A., Cohen M., Liu J., Han M., Wilson K.L., Gruenbaum Y.;
RT "Lamin-dependent localization of UNC-84, a protein required for nuclear
RT migration in Caenorhabditis elegans.";
RL Mol. Biol. Cell 13:892-901(2002).
RN [7]
RP FUNCTION, INTERACTION WITH UNC-83, SUBCELLULAR LOCATION, DOMAIN, AND
RP TOPOLOGY.
RX PubMed=16481402; DOI=10.1091/mbc.e05-09-0894;
RA McGee M.D., Rillo R., Anderson A.S., Starr D.A.;
RT "UNC-83 IS a KASH protein required for nuclear migration and is recruited
RT to the outer nuclear membrane by a physical interaction with the SUN
RT protein UNC-84.";
RL Mol. Biol. Cell 17:1790-1801(2006).
RN [8]
RP FUNCTION.
RX PubMed=20921138; DOI=10.1083/jcb.201004118;
RA Fridolfsson H.N., Starr D.A.;
RT "Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional
RT migrations of nuclei.";
RL J. Cell Biol. 191:115-128(2010).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF CYS-994.
RX PubMed=21798253; DOI=10.1016/j.ydbio.2011.07.008;
RA Xiong H., Mohler W.A., Soto M.C.;
RT "The branched actin nucleator Arp2/3 promotes nuclear migrations and cell
RT polarity in the C. elegans zygote.";
RL Dev. Biol. 357:356-369(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1-MET--ARG-208 AND
RP 118-TYR--LEU-244.
RX PubMed=21411627; DOI=10.1091/mbc.e10-08-0733;
RA Tapley E.C., Ly N., Starr D.A.;
RT "Multiple mechanisms actively target the SUN protein UNC-84 to the inner
RT nuclear membrane.";
RL Mol. Biol. Cell 22:1739-1752(2011).
RN [11]
RP FUNCTION.
RX PubMed=23150597; DOI=10.1534/genetics.112.146589;
RA Chang Y.T., Dranow D., Kuhn J., Meyerzon M., Ngo M., Ratner D.,
RA Warltier K., Starr D.A.;
RT "toca-1 is in a novel pathway that functions in parallel with a SUN-KASH
RT nuclear envelope bridge to move nuclei in Caenorhabditis elegans.";
RL Genetics 193:187-200(2013).
RN [12]
RP FUNCTION.
RX PubMed=25023515; DOI=10.1083/jcb.201405081;
RA Cain N.E., Tapley E.C., McDonald K.L., Cain B.M., Starr D.A.;
RT "The SUN protein UNC-84 is required only in force-bearing cells to maintain
RT nuclear envelope architecture.";
RL J. Cell Biol. 206:163-172(2014).
RN [13]
RP FUNCTION, INTERACTION WITH LMN-1, AND MUTAGENESIS OF 1-MET--ARG-208;
RP 40-LEU--LYS-161 AND PRO-91.
RX PubMed=25057012; DOI=10.1091/mbc.e14-05-0971;
RA Bone C.R., Tapley E.C., Gorjanacz M., Starr D.A.;
RT "The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to
RT transfer forces from the cytoplasm to the nucleoskeleton during nuclear
RT migration.";
RL Mol. Biol. Cell 25:2853-2865(2014).
RN [14]
RP FUNCTION, INTERACTION WITH ZYG-12, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP PRO-91; CYS-994 AND GLY-1002.
RX PubMed=27956467; DOI=10.1083/jcb.201604112;
RA Lawrence K.S., Tapley E.C., Cruz V.E., Li Q., Aung K., Hart K.C.,
RA Schwartz T.U., Starr D.A., Engebrecht J.;
RT "LINC complexes promote homologous recombination in part through inhibition
RT of nonhomologous end joining.";
RL J. Cell Biol. 215:801-821(2016).
CC -!- FUNCTION: Involved in nuclear migration and anchoring in hypodermal
CC precursor cells (PubMed:10375507, PubMed:11748140, PubMed:12169658,
CC PubMed:11907270, PubMed:16481402, PubMed:20921138, PubMed:21411627,
CC PubMed:23150597, PubMed:25023515, PubMed:25057012). Most likely
CC recruits anc-1 to the nuclear envelope where anc-1 functions to tether
CC the nucleus to the actin cytoskeleton (PubMed:12169658). Component of
CC the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton)
CC complex where it recruits and interacts with unc-83 to form a bridge
CC connecting the nuclear envelope to the cytoskeleton which allows for
CC nuclear transport along microtubules (PubMed:11748140,
CC PubMed:16481402). Its role in nuclear migration may be in association
CC with lamin, lmn-1 (PubMed:25057012). Regulates nuclear migrations in
CC one-cell embryos, controlling the posterior migration of the male
CC pronucleus following fertilization (PubMed:21798253). Not required for
CC centrosome attachment to the nucleus (PubMed:10375507,
CC PubMed:11907270). Plays a role in the maintenance of the nuclear
CC envelope architecture in body wall muscle cells (PubMed:25023515). May
CC be involved in DNA damage repair through an association with zyg-12
CC (PubMed:27956467). Potentially has roles in homologous recombination,
CC double strand break repair and meiotic recombination (PubMed:27956467).
CC Specifically, may in part inhibit non-homologous end joining repair,
CC most likely through recruiting fan-1 to the nucleoplasm, to facilitate
CC the repair of DNA cross-links (PubMed:27956467).
CC {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140,
CC ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:12169658,
CC ECO:0000269|PubMed:16481402, ECO:0000269|PubMed:20921138,
CC ECO:0000269|PubMed:21411627, ECO:0000269|PubMed:21798253,
CC ECO:0000269|PubMed:23150597, ECO:0000269|PubMed:25023515,
CC ECO:0000269|PubMed:25057012, ECO:0000269|PubMed:27956467}.
CC -!- SUBUNIT: Component of the unc-83-unc-84 LINC complex which contains at
CC least unc-83 and unc-84 (PubMed:11748140, PubMed:16481402). Within the
CC unc-83-unc-84 LINC complex interacts (via C-terminus) with unc-83; the
CC interaction is probably required to recruit unc-83 to the nuclear
CC membrane (PubMed:11748140, PubMed:16481402). Most likely interacts with
CC anc-1; the interaction is probably required to recruit anc-1 to the
CC nuclear envelope (PubMed:12169658). Interacts (via C-terminus) with
CC zyg-12 (via C-terminus); the interaction is direct (PubMed:27956467).
CC May interact with lmn-1; this interaction may be required to complete
CC the connection between the nuclear lamina and the cytoskeleton
CC (PubMed:25057012). {ECO:0000269|PubMed:11748140,
CC ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:16481402,
CC ECO:0000269|PubMed:25057012, ECO:0000269|PubMed:27956467}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:10375507, ECO:0000269|PubMed:11748140,
CC ECO:0000269|PubMed:11907270, ECO:0000269|PubMed:16481402,
CC ECO:0000269|PubMed:27956467, ECO:0000305|PubMed:21411627}; Single-pass
CC type II membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000305}. Note=Associated with nuclei during interphase, prophase,
CC prometaphase, metaphase and early anaphase (PubMed:11907270). Released
CC from nuclear membrane in the same time that the nuclear envelope
CC disassembly, during late anaphase, and begins to reaccumulate in early
CC telophase (PubMed:11907270). Localization at the nuclear envelope
CC depends on lmn-1 (PubMed:11748140, PubMed:11907270). Co-localizes with
CC unc-83 at the nuclear envelope, but its localization at the nuclear
CC envelope does not depend on unc-83 (PubMed:11748140, PubMed:11907270).
CC {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F54B11.3a}; Synonyms=L
CC {ECO:0000303|PubMed:11907270};
CC IsoId=Q20745-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F54B11.3b}; Synonyms=S
CC {ECO:0000303|PubMed:11907270};
CC IsoId=Q20745-2; Sequence=VSP_007081, VSP_007082;
CC -!- TISSUE SPECIFICITY: Expressed in all somatic cells (PubMed:11907270,
CC PubMed:27956467). Not expressed in germ cells in the mitotic and
CC transition zones of the gonad (PubMed:11907270). One study shows
CC expression at the beginning of the late pachytene stage in the proximal
CC gonad, but there is no expression in the male germline, suggesting
CC expression is specific to oogenesis in hermaphrodites
CC (PubMed:27956467). {ECO:0000269|PubMed:11907270,
CC ECO:0000269|PubMed:27956467}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all cells of embryos from the 26-cell
CC stage (PubMed:10375507, PubMed:11907270). Then, it is ubiquitously
CC expressed throughout the development (PubMed:10375507,
CC PubMed:11907270). Not expressed between fertilization and the 26-cell
CC stage (PubMed:11907270). {ECO:0000269|PubMed:10375507,
CC ECO:0000269|PubMed:11907270}.
CC -!- INDUCTION: Induced by DNA-damage. {ECO:0000269|PubMed:27956467}.
CC -!- DOMAIN: The SUN domain probably plays a role in the nuclear anchoring
CC and/or migration. Required for the localization of unc-83 and anc-1 at
CC the nuclear membrane. {ECO:0000269|PubMed:12169658,
CC ECO:0000269|PubMed:16481402}.
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DR EMBL; AF200706; AAF15883.1; -; mRNA.
DR EMBL; AF200707; AAF15884.1; -; mRNA.
DR EMBL; Z70208; CAA94142.2; -; Genomic_DNA.
DR EMBL; Z70208; CAC42306.1; -; Genomic_DNA.
DR PIR; T22608; T22608.
DR RefSeq; NP_001024707.1; NM_001029536.2. [Q20745-1]
DR RefSeq; NP_001024708.1; NM_001029537.3.
DR AlphaFoldDB; Q20745; -.
DR SMR; Q20745; -.
DR BioGRID; 46381; 11.
DR ComplexPortal; CPX-1385; unc-83-unc-84 LINC complex.
DR IntAct; Q20745; 5.
DR STRING; 6239.F54B11.3a; -.
DR iPTMnet; Q20745; -.
DR EPD; Q20745; -.
DR PaxDb; Q20745; -.
DR PeptideAtlas; Q20745; -.
DR EnsemblMetazoa; F54B11.3a.1; F54B11.3a.1; WBGene00006816. [Q20745-1]
DR EnsemblMetazoa; F54B11.3b.1; F54B11.3b.1; WBGene00006816. [Q20745-2]
DR GeneID; 181480; -.
DR KEGG; cel:CELE_F54B11.3; -.
DR UCSC; F54B11.3b.2; c. elegans. [Q20745-1]
DR CTD; 181480; -.
DR WormBase; F54B11.3a; CE28236; WBGene00006816; unc-84. [Q20745-1]
DR WormBase; F54B11.3b; CE27761; WBGene00006816; unc-84. [Q20745-2]
DR eggNOG; KOG2687; Eukaryota.
DR GeneTree; ENSGT00940000167324; -.
DR HOGENOM; CLU_009427_0_0_1; -.
DR InParanoid; Q20745; -.
DR OMA; HVITYIL; -.
DR OrthoDB; 266644at2759; -.
DR PRO; PR:Q20745; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006816; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:WormBase.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IPI:WormBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007399; P:nervous system development; IMP:WormBase.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IMP:WormBase.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; TAS:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Developmental protein;
KW Membrane; Nucleus; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1111
FT /note="Nuclear migration and anchoring protein unc-84"
FT /id="PRO_0000218910"
FT TOPO_DOM 1..509
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:16481402"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:21411627"
FT TOPO_DOM 531..1111
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:16481402"
FT DOMAIN 945..1109
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 118..244
FT /note="Required for nuclear envelope localization"
FT /evidence="ECO:0000269|PubMed:21411627"
FT REGION 232..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..507
FT /note="Required for nuclear envelope localization"
FT /evidence="ECO:0000269|PubMed:21411627"
FT REGION 912..1111
FT /note="Interaction with zyg-12"
FT /evidence="ECO:0000269|PubMed:27956467"
FT SITE 91
FT /note="May be involved in the interaction with lmn-1"
FT /evidence="ECO:0000269|PubMed:25057012"
FT VAR_SEQ 877..879
FT /note="LRA -> VTN (in isoform b)"
FT /evidence="ECO:0000303|PubMed:10375507"
FT /id="VSP_007081"
FT VAR_SEQ 880..1111
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:10375507"
FT /id="VSP_007082"
FT MUTAGEN 1..208
FT /note="Missing: In n322; defects in nuclear migration in
FT hyp7 hypodermal precursor cells. No nuclear envelope
FT localization defects in hyp7 precursor cells. Does not
FT affect the localization of unc-83 to the nuclear membrane
FT in embryos."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:21411627,
FT ECO:0000269|PubMed:25057012"
FT MUTAGEN 40..161
FT /note="Missing: In e1174; defects in nuclear migration in
FT distal tip cells and hyp7 hypodermal precursor cells."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:25057012"
FT MUTAGEN 91
FT /note="P->S: In e1411; defective nuclear migration in hyp7
FT hypodermal precursor cells. Does not affect unc-83
FT localization to the nuclear membrane in embryos. May reduce
FT interaction with lmn-1. Reduces number of viable progeny
FT following incubation with the DNA cross-linking agent
FT cisplatin."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:25057012,
FT ECO:0000269|PubMed:27956467, ECO:0000305|PubMed:12169658"
FT MUTAGEN 118..244
FT /note="Missing: Abolishes localization to the nuclear
FT envelope of hyp7 precursor cells."
FT /evidence="ECO:0000269|PubMed:21411627"
FT MUTAGEN 932
FT /note="D->N: In n323; defective nuclear migration and
FT anchoring in hyp7 hypodermal precursor cells. No defects in
FT localization to the nuclear envelope, however unc-83
FT localization to the nuclear envelope is abolished."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270"
FT MUTAGEN 984
FT /note="R->K: In n371; defects in nuclear migration and
FT anchoring in hyp7 hypodermal precursor cells. No defects in
FT localization to the nuclear envelope, however unc-83
FT localization to the nuclear envelope is abolished."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270"
FT MUTAGEN 988
FT /note="S->F: In sa61; defects in nuclear migration and
FT anchoring in hyp7 hypodermal precursor cells. No defects in
FT localization to the nuclear envelope, however unc-83
FT localization to the nuclear envelope is abolished."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270"
FT MUTAGEN 994
FT /note="C->Y: In e1410; defects in nuclear migration and
FT anchoring in hyp7 hypodermal precursor cells. Defective
FT male pronuclear migration in one-cell embryos following
FT fertilization. Reduced number of viable progeny following
FT incubation with the DNA cross-linking agent cisplatin."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:21798253, ECO:0000269|PubMed:27956467"
FT MUTAGEN 1002
FT /note="G->D: In n321 and n399; defects in nuclear migration
FT and anchoring in hyp7 hypodermal precursor cells. No
FT defects in localization to the nuclear envelope, however
FT unc-83 localization to the nuclear envelope is abolished.
FT Reduced number of viable progeny following incubation with
FT the DNA cross-linking agent cisplatin."
FT /evidence="ECO:0000269|PubMed:10375507,
FT ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:11907270,
FT ECO:0000269|PubMed:12169658, ECO:0000269|PubMed:27956467"
SQ SEQUENCE 1111 AA; 125861 MW; 6A07438E2BDC8BA6 CRC64;
MAPATEADNN FDTHEWKSEF ASTRSGRNSP NIFAKVRRKL LLTPPVRNAR SPRLTEEELD
ALTGDLPYAT NYTYAYSKIY DPSLPDHWEV PNLGGTTSGS LSEQEHWSAA SLSRQLLYIL
RFPVYLVLHV ITYILEAFYH VIKITSFTIW DYLLYLVKLA KTRYYAYQDH RRRTALIRNR
QEPFSTKAAR SIRRFFEILV YVVLTPYRML TRSNNGVEQY QYRSIKDQLE NERASRMTTR
SQTLERSRKF DGLSKSPARR AAPAFVKTST ITRITAKVFS SSPFGEGTSE NITPTVVTTR
TVKQRSVTPR FRQTRATREA ITRALDTPEL EIDTPLSTYG LRSRGLSHLN TPEPTFDIGH
AAATSTPLFP QETYNYQYEE ATGNKIKTAF TWLGYLILFP FFAARHVWYT FYDYGKSAYM
KLTNYQQAPM ETIHVRDINE PAPSSSDVHD AVGVSWRIRI ADFLSSFVAT IVEAHQVVFA
MFKGGIVETV SYFGGLFAGL TDKKSSKFSW CQILGLLLAL LFAIFLLGFL TSDNTAIRVK
EITKDKNASK KSEGSLPAVP IWISAANHVK HYTWMVKEFV VDIAFDTYNY GKSTIGRLGT
TPRYAWDLIA SGCGAVGNGL KSVLSSSFRF IDFCAGKLFY YGSDGFLSAN KSIGTFFNGC
YETLYNGCTA IVGHTKSFIY NASNAVYNFF STIFAGLLNF STSSQNSILS LLKSFGTGIT
NIFYNFIYAP IAGVFNFAGD NYMYFFNEVA AVFGKVYNSV VSVLKTVINW ILFLIAYPFS
LCTRAWIRIS QYAPEDVVQV IPIPQAITPT PDVERIVEEP LRKVTDVEDE ELVIIPAPAP
KPIPVPAPTP APVIIHQTNV VETVDKDAII KEVTEKLRAE LSAQFQQELS AKFEQNYNTI
IEQLKMENTN IQYDKNHLEA IIRQMIYEYD TDKTGKVDYA LESSGGAVVS TRCSETYKSY
TRLEKFWDIP IYYFHYSPRV VIQRNSKSLF PGECWCFKES RGYIAVELSH FIDVSSISYE
HIGSEVAPEG NRSSAPKGVL VWAYKQIDDL NSRVLIGDYT YDLDGPPLQF FLAKHKPDFP
VKFVELEVTS NYGAPFTCLY RLRVHGKVVQ V
