MTCL1_MOUSE
ID MTCL1_MOUSE Reviewed; 1945 AA.
AC Q3UHU5; Q6PAM2; Q80TR7;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Microtubule cross-linking factor 1;
DE AltName: Full=Coiled-coil domain-containing protein 165;
DE AltName: Full=PAR-1-interacting protein;
DE AltName: Full=SOGA family member 2;
GN Name=Mtcl1; Synonyms=Ccdc165, Kiaa0802, Soga2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1362-1913 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-213; SER-255;
RP SER-290; SER-768; THR-1403; SER-1407; SER-1799 AND SER-1801, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH MARK2, SUBUNIT, ASSOCIATION WITH MICROTUBULES,
RP AND SUBCELLULAR LOCATION.
RX PubMed=23902687; DOI=10.1242/jcs.127845;
RA Sato Y., Akitsu M., Amano Y., Yamashita K., Ide M., Shimada K.,
RA Yamashita A., Hirano H., Arakawa N., Maki T., Hayashi I., Ohno S.,
RA Suzuki A.;
RT "The novel PAR-1-binding protein MTCL1 has crucial roles in organizing
RT microtubules in polarizing epithelial cells.";
RL J. Cell Sci. 126:4671-4683(2013).
CC -!- FUNCTION: Microtubule-associated factor involved in the late phase of
CC epithelial polarization and microtubule dynamics regulation. Plays a
CC role in the development and maintenance of non-centrosomal microtubule
CC bundles at the lateral membrane in polarized epithelial cells.
CC {ECO:0000269|PubMed:23902687}.
CC -!- SUBUNIT: Homodimer. Isoform 1 interacts with MARK2; the interaction
CC increases MARK2 microtubule-binding ability. Associates (via N- and C-
CC terminus domains) with microtubule filaments.
CC {ECO:0000269|PubMed:23902687}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Lateral cell membrane. Apical cell
CC membrane. Cytoplasm, cytoskeleton, spindle pole. Midbody. Cytoplasm,
CC cytoskeleton. Note=Colocalized with microtubules at the base of cilia.
CC Gradually accumulates on the apicobasal microtubule bundles during
CC epithelial cell polarization (By similarity). Colocalized with the
CC apicobasal microtubule bundles running beneath the lateral membrane.
CC Colocalized with microtubule bundles in the spindle pole in mitotic
CC cells and in the midbodies at the end of cytokinesis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UHU5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHU5-2; Sequence=VSP_023555;
CC Name=3;
CC IsoId=Q3UHU5-3; Sequence=VSP_023556;
CC -!- SIMILARITY: Belongs to the SOGA family. {ECO:0000305}.
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DR EMBL; AK147205; BAE27762.1; -; mRNA.
DR EMBL; BC060225; AAH60225.1; -; mRNA.
DR EMBL; AK122373; BAC65655.1; -; mRNA.
DR CCDS; CCDS28946.2; -. [Q3UHU5-1]
DR CCDS; CCDS50168.1; -. [Q3UHU5-3]
DR RefSeq; NP_001107570.1; NM_001114098.1. [Q3UHU5-3]
DR RefSeq; NP_766551.3; NM_172963.4. [Q3UHU5-1]
DR AlphaFoldDB; Q3UHU5; -.
DR SMR; Q3UHU5; -.
DR BioGRID; 212955; 3.
DR IntAct; Q3UHU5; 1.
DR STRING; 10090.ENSMUSP00000083899; -.
DR iPTMnet; Q3UHU5; -.
DR PhosphoSitePlus; Q3UHU5; -.
DR EPD; Q3UHU5; -.
DR MaxQB; Q3UHU5; -.
DR PaxDb; Q3UHU5; -.
DR PeptideAtlas; Q3UHU5; -.
DR PRIDE; Q3UHU5; -.
DR ProteomicsDB; 287627; -. [Q3UHU5-1]
DR ProteomicsDB; 287628; -. [Q3UHU5-2]
DR ProteomicsDB; 287629; -. [Q3UHU5-3]
DR Antibodypedia; 48434; 33 antibodies from 14 providers.
DR Ensembl; ENSMUST00000086693; ENSMUSP00000083899; ENSMUSG00000052105. [Q3UHU5-1]
DR Ensembl; ENSMUST00000097291; ENSMUSP00000094894; ENSMUSG00000052105. [Q3UHU5-3]
DR GeneID; 68617; -.
DR KEGG; mmu:68617; -.
DR UCSC; uc008djv.2; mouse. [Q3UHU5-3]
DR UCSC; uc008djw.2; mouse. [Q3UHU5-1]
DR CTD; 23255; -.
DR MGI; MGI:1915867; Mtcl1.
DR VEuPathDB; HostDB:ENSMUSG00000052105; -.
DR eggNOG; KOG4787; Eukaryota.
DR GeneTree; ENSGT00950000182982; -.
DR HOGENOM; CLU_002595_0_0_1; -.
DR InParanoid; Q3UHU5; -.
DR OMA; KDLHARP; -.
DR OrthoDB; 34629at2759; -.
DR PhylomeDB; Q3UHU5; -.
DR TreeFam; TF331853; -.
DR BioGRID-ORCS; 68617; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Mtcl1; mouse.
DR PRO; PR:Q3UHU5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3UHU5; protein.
DR Bgee; ENSMUSG00000052105; Expressed in retinal neural layer and 242 other tissues.
DR ExpressionAtlas; Q3UHU5; baseline and differential.
DR Genevisible; Q3UHU5; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0097427; C:microtubule bundle; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
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; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1945
FT /note="Microtubule cross-linking factor 1"
FT /id="PRO_0000280114"
FT REGION 1..500
FT /note="Necessary for self-assembly, microtubule bundling
FT activity and apicobasal microtubule organization"
FT REGION 1..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..241
FT /note="Necessary for colocalization and binding with
FT microtubules"
FT REGION 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1368
FT /note="Necessary for interaction with MARK2 and apicobasal
FT microtubule bundle formation in polarized epithelial cells"
FT /evidence="ECO:0000250"
FT REGION 1272..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1767
FT /note="Necessary for colocalization and binding with
FT microtubules"
FT /evidence="ECO:0000250"
FT REGION 1701..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..396
FT /evidence="ECO:0000255"
FT COILED 424..712
FT /evidence="ECO:0000255"
FT COILED 1120..1196
FT /evidence="ECO:0000255"
FT COILED 1229..1270
FT /evidence="ECO:0000255"
FT COMPBIAS 21..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1913..1927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1413
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1661
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B5"
FT MOD_RES 1799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..514
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023555"
FT VAR_SEQ 1882..1945
FT /note="ELPCSALAPSLEPCFSRPERPANRRLPSRWAPPSPTASQSQSPGHPMSMEEH
FT GEEDPPEEKPHL -> NQTVLLTAPWGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_023556"
SQ SEQUENCE 1945 AA; 213862 MW; 7785C70146349A03 CRC64;
METLNGPAGG GAPDTKPQPA GQHHRHHHLH PLAERRRLHR APSPARPFLK DLHTRPATAT
PSAGRAPTPA APRSPSLAGK APPSPGPPAA PGRLSRRSGV VPGAKDKPPP GAGARSAGGA
KAVPGTRRAA RAGPAEPLSR VGRPTGAEPP PAVAKGRKTK RGPGTPPARA VVPPARASRV
PAVTLSVTSV AGCRINHTDS SSDLSDCASE PLSDEQRLLP AASSDAESGT GSSDREPIRG
APTPSSGSRG PPPGSPEPPI LLAAPPVASA CLGGRSSPGG ASTGSPGPGS QEDVGGRAPP
ERTILGTSKE PSLGEQPRLL VVAEEEELLR EMEELRSEND YLKDELDELR AEMEEMRDSY
LEEDGYQLQE LRRELDRANK NCRILQYRLR KAEQKSLKVA ETGQVDGELI RSLEQDLKVA
KDVSVRLHHE LETVEEKRAK AEDDNETLRQ QMIEVEVSRQ ALQNEVERLR ESSLKRRGSR
EMYKEKKLVN QDDSADLKCQ LQFVKEEASL MRKKMAKLGR EKDELEQELQ KYKSLYGDVD
SPLPTGEAGG PPSTREAELK LRLKLVEEEA SILGRKIVEL EVENRGLKAE MEDIRVQHER
EGTGRDHVPS TPTSPFGDSM ESSTELRRHL QFVEEEAELL RRSISEIEDH NRQLTHELSK
FKFEPHQESG WLGDGVSKGP AASVPLQEEL KSARLQIDEL SGKVLKLQCE NRLLLSNAQR
GDLAAHLGLR APSPRDSDAE SDAGKKESDG EEGRLPQPKR EGPVGGESDS EDMFEKTSGF
GSGKPSEASE PCPAELLRVR EDTECLVTIK LEAQRLERTV ERLISDTDGF IHDSGLRGNG
LASPGVQGGG GEGNSPSEPH LLETINVRMK AFRKELQAFL EQMSRIVDGL SPLSHLTESS
SFLSTVTSVS RDSPIGTLGK ELGPDLQSKL REQLEWQLNQ DRGDEREGLR LRATRELHRR
ADGDSGSHHG LGGQSCFNLE MEEDHLYALR WKELEMHSLA LQNTLHKRTW SDEKNLLQQE
LRSLKQNIFL FYVKLRWLLK HWRQGKQMEE GGEDLEESEH PENVPGLAEL GVQGVHQTDG
IDQEDADQGC SLPMGEHAPH SLVQISEHGS RLQSSDGGPL NKQVVENQQL FRALKALLED
FRSELREDEH ARLRLQQQYA SDKAAWDVEW AVLKCRLEQL EEKTEKSLGE LDSSAEGKGA
LKKEREVHQK LLADSHSLVM DLRWQIHHRE KNWNREKVEL LERLDSERQE WGRQKEELLW
RVEQLQKEKS PRRSGSFLCS RREDDTRPYP HQGSLHSSRP VSMWPCEDAD SIPFEDRPLS
KLKESDRCSA SENLYLDALS LDDDPGDPPP LRNCLAEEEE SRKGNLQRAV SVSCMSEFQR
LMDVSPFLPE KGLPSAGSKE DVTPPLSPDD LKYIEEFHSN DWDYASPRAE ADRPPDPWAD
RTEMGRVGHE ATTEPCPDPS WYLTTSVTMT TDTMTSPEHC QKQPLRTHVL TEQSGVHVLH
SPPAIRRVDS IASGGEGRSR ADPEGPFPMS RARGNLADAK GGHPEPVLNR WPCTPPRHPR
DCVEGSLRPL DRPICPSLGF ASPLNSLDMS KNMSDDMKEV AFSVRNAICA GPAEPHVRDM
ACQTNGSRTA GTQTIQTISV GLQTEALRAS GVTSSPHKCL TPKAGGGTTP VSSPSRSLRS
RQVAPAIEKV QAKFERTCCS PKYGSPKLQR KPLSKADQPN SRTSPGIPQK GFSESAWARS
TTTRESPVHT TINDGLSSLF NIIDHSPIGV RAGSRSRSAE PRQELGPGQE TGTSSRGRSP
SPLGVGSETF REEGGESTPV RQDLSAPPGY TLTENVARIL NKKLLEHALK EERKQASHGS
SGLTSDSHTG EPVPAEPGSM EELPCSALAP SLEPCFSRPE RPANRRLPSR WAPPSPTASQ
SQSPGHPMSM EEHGEEDPPE EKPHL
