SYNE3_HUMAN
ID SYNE3_HUMAN Reviewed; 975 AA.
AC Q6ZMZ3; A6H8H3; Q86SX5; Q8N7G8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Nesprin-3;
DE AltName: Full=KASH domain-containing protein 3;
DE Short=KASH3;
DE AltName: Full=Nuclear envelope spectrin repeat protein 3;
GN Name=SYNE3 {ECO:0000312|HGNC:HGNC:19861};
GN Synonyms=C14orf139 {ECO:0000312|HGNC:HGNC:19861},
GN C14orf49 {ECO:0000312|HGNC:HGNC:19861},
GN LINC00341 {ECO:0000312|HGNC:HGNC:19861};
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=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-668
RP AND LEU-795 DEL.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-975 (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 411-975 (ISOFORM 1), AND VARIANTS MET-668
RP AND VAL-923.
RC TISSUE=Synovial cell, and Thyroid;
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 FUNCTION.
RX PubMed=16330710; DOI=10.1083/jcb.200506083;
RA Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N., Janssen H.,
RA van den Bout I., Raymond K., Sonnenberg A.;
RT "Nesprin-3, a novel outer nuclear membrane protein, associates with the
RT cytoskeletal linker protein plectin.";
RL J. Cell Biol. 171:799-810(2005).
RN [6]
RP FUNCTION, DOMAIN, AND INTERACTION WITH SUN1 AND SUN2.
RX PubMed=18396275; DOI=10.1016/j.yexcr.2008.02.022;
RA Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.;
RT "Structural requirements for the assembly of LINC complexes and their
RT function in cellular mechanical stiffness.";
RL Exp. Cell Res. 314:1892-1905(2008).
RN [7]
RP INTERACTION WITH TOR1A.
RX PubMed=18827015; DOI=10.1242/jcs.029454;
RA Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y.,
RA Wiche G., Sonnenberg A., Breakefield X.O.;
RT "TorsinA binds the KASH domain of nesprins and participates in linkage
RT between nuclear envelope and cytoskeleton.";
RL J. Cell Sci. 121:3476-3486(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21937718; DOI=10.1091/mbc.e11-04-0287;
RA Morgan J.T., Pfeiffer E.R., Thirkill T.L., Kumar P., Peng G.,
RA Fridolfsson H.N., Douglas G.C., Starr D.A., Barakat A.I.;
RT "Nesprin-3 regulates endothelial cell morphology, perinuclear cytoskeletal
RT architecture, and flow-induced polarization.";
RL Mol. Biol. Cell 22:4324-4334(2011).
RN [10]
RP INTERACTION WITH SYNE1.
RX PubMed=22518138; DOI=10.1155/2012/736524;
RA Taranum S., Sur I., Muller R., Lu W., Rashmi R.N., Munck M., Neumann S.,
RA Karakesisoglou I., Noegel A.A.;
RT "Cytoskeletal interactions at the nuclear envelope mediated by nesprins.";
RL Int. J. Cell Biol. 2012:736524-736524(2012).
CC -!- FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and
CC Cytoskeleton) complex involved in the connection between the nuclear
CC lamina and the cytoskeleton. The nucleocytoplasmic interactions
CC established by the LINC complex play an important role in the
CC transmission of mechanical forces across the nuclear envelope and in
CC nuclear movement and positioning. Probable anchoring protein which
CC tethers the nucleus to the cytoskeleton by binding PLEC which can
CC associate with the intermediate filament system. Plays a role in the
CC regulation of aortic epithelial cell morphology, and is required for
CC flow-induced centrosome polarization and directional migration in
CC aortic endothelial cells. {ECO:0000269|PubMed:16330710,
CC ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:21937718}.
CC -!- SUBUNIT: Core component of LINC complexes which are composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC containing proteins seem to bind each other promiscuously; however,
CC differentially expression of LINC complex constituents can give rise to
CC specific assemblies. Interacts with SUN1 and SUN2; probably forming
CC respective LINC complexes. Interacts with PLEC (via actin-binding
CC domain). Interacts with DST. Interacts with SYNE1 via spectrin repeats.
CC Interacts (via KASH domain) with TOR1A (ATP-bound); the interaction is
CC required for SYNE3 nuclear envelope localization.
CC {ECO:0000269|PubMed:18396275, ECO:0000269|PubMed:18827015,
CC ECO:0000269|PubMed:22518138}.
CC -!- INTERACTION:
CC Q6ZMZ3-1; Q6ZWR6-5: Syne1; Xeno; NbExp=2; IntAct=EBI-10760907, EBI-10760805;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:21937718}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:21937718}. Nucleus envelope
CC {ECO:0000269|PubMed:21937718}. Rough endoplasmic reticulum
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q6ZMZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMZ3-2; Sequence=VSP_023978;
CC Name=3;
CC IsoId=Q6ZMZ3-3; Sequence=VSP_023976, VSP_023977;
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein
CC level). {ECO:0000269|PubMed:21937718}.
CC -!- DOMAIN: The KASH domain is involved in the binding to SUN1 and SUN2
CC through recognition of their SUN domains.
CC {ECO:0000269|PubMed:18396275}.
CC -!- PTM: The disulfid bond with SUN1 or SUN2 is required for stability of
CC the respective LINC complex under tensile forces.
CC {ECO:0000250|UniProtKB:Q8WXH0}.
CC -!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05312.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD18582.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD62365.1; Type=Erroneous initiation; Note=Extended 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; BX248076; CAD62365.1; ALT_INIT; mRNA.
DR EMBL; AL138539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146604; AAI46605.1; -; mRNA.
DR EMBL; AK098471; BAC05312.1; ALT_INIT; mRNA.
DR EMBL; AK131436; BAD18582.1; ALT_INIT; mRNA.
DR CCDS; CCDS86430.1; -. [Q6ZMZ3-2]
DR CCDS; CCDS9935.1; -. [Q6ZMZ3-1]
DR RefSeq; NP_689805.3; NM_152592.4. [Q6ZMZ3-1]
DR RefSeq; XP_005267434.1; XM_005267377.3.
DR RefSeq; XP_006720126.1; XM_006720063.3. [Q6ZMZ3-1]
DR RefSeq; XP_016876545.1; XM_017021056.1.
DR PDB; 6WME; X-ray; 1.53 A; B=948-975.
DR PDBsum; 6WME; -.
DR AlphaFoldDB; Q6ZMZ3; -.
DR SMR; Q6ZMZ3; -.
DR BioGRID; 127775; 433.
DR IntAct; Q6ZMZ3; 2.
DR STRING; 9606.ENSP00000334308; -.
DR CarbonylDB; Q6ZMZ3; -.
DR iPTMnet; Q6ZMZ3; -.
DR PhosphoSitePlus; Q6ZMZ3; -.
DR SwissPalm; Q6ZMZ3; -.
DR BioMuta; SYNE3; -.
DR DMDM; 134035037; -.
DR EPD; Q6ZMZ3; -.
DR jPOST; Q6ZMZ3; -.
DR MassIVE; Q6ZMZ3; -.
DR MaxQB; Q6ZMZ3; -.
DR PaxDb; Q6ZMZ3; -.
DR PeptideAtlas; Q6ZMZ3; -.
DR PRIDE; Q6ZMZ3; -.
DR ProteomicsDB; 67943; -. [Q6ZMZ3-1]
DR ProteomicsDB; 67944; -. [Q6ZMZ3-2]
DR ProteomicsDB; 67945; -. [Q6ZMZ3-3]
DR Antibodypedia; 54248; 161 antibodies from 28 providers.
DR DNASU; 161176; -.
DR Ensembl; ENST00000334258.9; ENSP00000334308.4; ENSG00000176438.13. [Q6ZMZ3-1]
DR Ensembl; ENST00000553340.1; ENSP00000450774.1; ENSG00000176438.13. [Q6ZMZ3-3]
DR Ensembl; ENST00000557275.5; ENSP00000450562.1; ENSG00000176438.13. [Q6ZMZ3-2]
DR Ensembl; ENST00000682763.1; ENSP00000507501.1; ENSG00000176438.13. [Q6ZMZ3-1]
DR GeneID; 161176; -.
DR KEGG; hsa:161176; -.
DR MANE-Select; ENST00000682763.1; ENSP00000507501.1; NM_152592.6; NP_689805.3.
DR UCSC; uc001yei.4; human. [Q6ZMZ3-1]
DR CTD; 161176; -.
DR DisGeNET; 161176; -.
DR GeneCards; SYNE3; -.
DR HGNC; HGNC:19861; SYNE3.
DR HPA; ENSG00000176438; Low tissue specificity.
DR MIM; 610861; gene.
DR neXtProt; NX_Q6ZMZ3; -.
DR OpenTargets; ENSG00000176438; -.
DR PharmGKB; PA134931380; -.
DR VEuPathDB; HostDB:ENSG00000176438; -.
DR eggNOG; ENOG502QQSI; Eukaryota.
DR GeneTree; ENSGT00440000039367; -.
DR HOGENOM; CLU_012764_0_0_1; -.
DR InParanoid; Q6ZMZ3; -.
DR OMA; KICRLEP; -.
DR OrthoDB; 87219at2759; -.
DR PhylomeDB; Q6ZMZ3; -.
DR TreeFam; TF331132; -.
DR PathwayCommons; Q6ZMZ3; -.
DR SignaLink; Q6ZMZ3; -.
DR SIGNOR; Q6ZMZ3; -.
DR BioGRID-ORCS; 161176; 5 hits in 1068 CRISPR screens.
DR ChiTaRS; SYNE3; human.
DR GenomeRNAi; 161176; -.
DR Pharos; Q6ZMZ3; Tbio.
DR PRO; PR:Q6ZMZ3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q6ZMZ3; protein.
DR Bgee; ENSG00000176438; Expressed in tendon of biceps brachii and 191 other tissues.
DR ExpressionAtlas; Q6ZMZ3; baseline and differential.
DR Genevisible; Q6ZMZ3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005640; C:nuclear outer membrane; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0140444; F:cytoskeleton-nuclear membrane anchor activity; IDA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IDA:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR InterPro; IPR012315; KASH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR030267; SYNE3.
DR PANTHER; PTHR47535:SF2; PTHR47535:SF2; 1.
DR Pfam; PF10541; KASH; 1.
DR Pfam; PF00435; Spectrin; 1.
DR SMART; SM01249; KASH; 1.
DR SMART; SM00150; SPEC; 3.
DR PROSITE; PS51049; KASH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Nucleus; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..975
FT /note="Nesprin-3"
FT /id="PRO_0000281120"
FT TOPO_DOM 1..925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TRANSMEM 926..946
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TOPO_DOM 947..975
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT REPEAT 220..325
FT /note="Spectrin 1"
FT REPEAT 647..740
FT /note="Spectrin 2"
FT DOMAIN 917..975
FT /note="KASH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT COILED 617..645
FT /evidence="ECO:0000255"
FT DISULFID 953
FT /note="Interchain (C-563 in SUN2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT DISULFID 953
FT /note="Interchain (with C-657 in SUN1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT VAR_SEQ 593..596
FT /note="GLQE -> VRGL (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023976"
FT VAR_SEQ 597..975
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023977"
FT VAR_SEQ 793..797
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023978"
FT VARIANT 668
FT /note="T -> M (in dbSNP:rs9671369)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031231"
FT VARIANT 795
FT /note="Missing (in dbSNP:rs76499929)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_068433"
FT VARIANT 864
FT /note="R -> H (in dbSNP:rs17092216)"
FT /id="VAR_031232"
FT VARIANT 923
FT /note="A -> V (in dbSNP:rs12434757)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031233"
FT VARIANT 946
FT /note="I -> V (in dbSNP:rs10130647)"
FT /id="VAR_031234"
FT STRAND 966..971
FT /evidence="ECO:0007829|PDB:6WME"
SQ SEQUENCE 975 AA; 112216 MW; A409AF86E1E781F4 CRC64;
MTQQPQDDFD RSVEDAQAWM KAVQDQLQVN DNTQGPRAAL EARLWETEKI CQLEPEGRVR
VDLVLRMAEA LLACCPGDQK PGILARLKDI KAQWEETVTY MTHCHSRIEW VWLHWSEYLL
ARDEFYRWFQ KMMVTLEPHI ELQLGLKEKQ WQLSHAQVLL HNVDNQAVLL DRLLEEAASL
FNRIGDPSVD EDAQKRMKAE YDAVKAKAQK RVDLLEQVAR EHEEYQAGVD EFQLWLKAVV
EKVNGCLGRN CKLPITQRLS TLQDIAKDFP RGEESLETLE EQSAGVIRNT SPLGAEKITG
ELEEMRKVLE KLRALWEEEE ERLRGLLRSR GAWEQQIKQL EAELSEFRMV LQRLAQEGLQ
PAAKAGTEDE LVAHWRRYSA TRAALASEEP RVDRLQAQLK ELIVFPHNLK PLSDSVIATI
QEYQSLKVKS ARLRNAAAVE LWQHFQRPLQ DLQLWKALAQ RLLEVTASLP DLPSLHTFLP
QIEAALMESS RLKELLTMLQ LKKDLLIGIF GQERATALLE QVAGSMRDRD LLHNSLLQRK
SKLQSLLAQH KDFGAAFEPL QRKLLDLQVR VQAEKGLQRD LPGKQAQLSR LQGLQEEGLD
LGAQMEAARP LVQENPNHQH KMDQLSSDFQ ALQRSLEDLV DRCRQSVQEH CTFSHQLLEL
RQWIVVTTQK LEAHRGEAGP GDAESQEAEF ERLVAEFPEK EAQLSLVEAQ GWLVMEKSSP
EGAAVVQEEL RELAESWRAL RLLEESLLSL IRNWHLQRME VDSGKKMVFT NNIPKSGFLI
NPMDPIPRHR RRANLLQEEE GSHEDFSQLL RNFGQWLQVE NSKLVRIIAM RTSTAEDLRT
RKSKLQELEA RVPEGQHLFE NLLRLGPARG TSDELEDLRY QWMLYKSKLK DSGHLLTQSS
PGEPTGFQKT RRWRGLGSLF RRACCVALPL QLLLLLFLLL LFLLPIREED RSCTLANNFA
RSFTLMLRYN GPPPT
