TM201_HUMAN
ID TM201_HUMAN Reviewed; 666 AA.
AC Q5SNT2; B9EH90; Q5SNT3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transmembrane protein 201;
DE AltName: Full=Spindle-associated membrane protein 1;
GN Name=TMEM201; Synonyms=NET5, SAMP1;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454 AND SER-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP FUNCTION (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX PubMed=19494128; DOI=10.1242/jcs.047373;
RA Buch C., Lindberg R., Figueroa R., Gudise S., Onischenko E., Hallberg E.;
RT "An integral protein of the inner nuclear membrane localizes to the mitotic
RT spindle in mammalian cells.";
RL J. Cell Sci. 122:2100-2107(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY
RP 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 [7]
RP SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYS-48 AND CYS-121,
RP INTERACTION WITH EMD, AND FUNCTION.
RX PubMed=21610090; DOI=10.1242/jcs.078923;
RA Gudise S., Figueroa R.A., Lindberg R., Larsson V., Hallberg E.;
RT "Samp1 is functionally associated with the LINC complex and A-type lamina
RT networks.";
RL J. Cell Sci. 124:2077-2085(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-444; SER-450;
RP SER-454; SER-466; SER-477 AND SER-480, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=27541860; DOI=10.1080/19491034.2016.1220465;
RA Vijayaraghavan B., Jafferali M.H., Figueroa R.A., Hallberg E.;
RT "Samp1, a RanGTP binding transmembrane protein in the inner nuclear
RT membrane.";
RL Nucleus 7:415-423(2016).
CC -!- FUNCTION: Involved in nuclear movement during fibroblast polarization
CC and migration. Proposed to be involved in actin-dependent nuclear
CC movement via association with transmembrane actin-associated nuclear
CC (TAN) lines which are bound to F-actin cables and couple the nucleus to
CC retrograde actin flow (By similarity). Overexpression can recruit Ran
CC GTPase to the nuclear periphery (PubMed:27541860).
CC {ECO:0000250|UniProtKB:A2A8U2, ECO:0000305|PubMed:27541860}.
CC -!- FUNCTION: [Isoform 2]: May define a distinct membrane domain in the
CC vicinity of the mitotic spindle (PubMed:19494128). Involved in the
CC organization of the nuclear envelope implicating EMD, SUN1 and A-type
CC lamina (PubMed:21610090). {ECO:0000269|PubMed:19494128,
CC ECO:0000269|PubMed:21610090}.
CC -!- SUBUNIT: Isoform 2 interacts with EMD (PubMed:21610090). Interacts with
CC SUN2 and LMNA (By similarity). May bind to Ran GTPase; has a greater
CC affinity for Ran-GTP over Ran-GDP. {ECO:0000250|UniProtKB:A2A8U2,
CC ECO:0000269|PubMed:21610090, ECO:0000305|PubMed:27541860}.
CC -!- INTERACTION:
CC Q5SNT2-2; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-11994282, EBI-11977093;
CC Q5SNT2-2; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-11994282, EBI-18013275;
CC Q5SNT2-2; P00387: CYB5R3; NbExp=3; IntAct=EBI-11994282, EBI-1046040;
CC Q5SNT2-2; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-11994282, EBI-296550;
CC Q5SNT2-2; P50402: EMD; NbExp=4; IntAct=EBI-11994282, EBI-489887;
CC Q5SNT2-2; Q969F0: FATE1; NbExp=3; IntAct=EBI-11994282, EBI-743099;
CC Q5SNT2-2; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-11994282, EBI-6911547;
CC Q5SNT2-2; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11994282, EBI-13345167;
CC Q5SNT2-2; Q92806: KCNJ9; NbExp=3; IntAct=EBI-11994282, EBI-12822837;
CC Q5SNT2-2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-11994282, EBI-2820517;
CC Q5SNT2-2; Q8N386: LRRC25; NbExp=3; IntAct=EBI-11994282, EBI-11304917;
CC Q5SNT2-2; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-11994282, EBI-11956541;
CC Q5SNT2-2; Q9UPX6: MINAR1; NbExp=3; IntAct=EBI-11994282, EBI-11977115;
CC Q5SNT2-2; Q8N183: NDUFAF2; NbExp=3; IntAct=EBI-11994282, EBI-2682365;
CC Q5SNT2-2; P54829: PTPN5; NbExp=3; IntAct=EBI-11994282, EBI-1220572;
CC Q5SNT2-2; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-11994282, EBI-12814225;
CC Q5SNT2-2; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-11994282, EBI-10982110;
CC Q5SNT2-2; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-11994282, EBI-11722971;
CC Q5SNT2-2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-11994282, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane
CC {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19494128}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:19494128}. Note=The C-
CC terminal of isoform 2 is located on the nucleoplasmic side. During
CC interphase, isoform 2 is distributed in the inner nuclear membrane in
CC distinct micro-domains and during mitosis, it is found in the ER but it
CC also localizes to the polar regions of the mitotic spindle.
CC {ECO:0000269|PubMed:19494128, ECO:0000269|PubMed:21610090}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SNT2-1; Sequence=Displayed;
CC Name=2; Synonyms=SAMP1;
CC IsoId=Q5SNT2-2; Sequence=VSP_030915, VSP_030916;
CC -!- SIMILARITY: Belongs to the TMEM201 family. {ECO:0000305}.
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DR EMBL; AL954705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121187; AAI21188.1; -; mRNA.
DR EMBL; BC137291; AAI37292.1; -; mRNA.
DR CCDS; CCDS30579.1; -. [Q5SNT2-2]
DR CCDS; CCDS44055.2; -. [Q5SNT2-1]
DR RefSeq; NP_001010866.1; NM_001010866.3. [Q5SNT2-2]
DR RefSeq; NP_001124396.2; NM_001130924.2. [Q5SNT2-1]
DR RefSeq; XP_011539212.1; XM_011540910.2. [Q5SNT2-2]
DR AlphaFoldDB; Q5SNT2; -.
DR SMR; Q5SNT2; -.
DR BioGRID; 128285; 171.
DR IntAct; Q5SNT2; 28.
DR STRING; 9606.ENSP00000344503; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR iPTMnet; Q5SNT2; -.
DR PhosphoSitePlus; Q5SNT2; -.
DR SwissPalm; Q5SNT2; -.
DR BioMuta; TMEM201; -.
DR DMDM; 74743441; -.
DR EPD; Q5SNT2; -.
DR jPOST; Q5SNT2; -.
DR MassIVE; Q5SNT2; -.
DR MaxQB; Q5SNT2; -.
DR PaxDb; Q5SNT2; -.
DR PeptideAtlas; Q5SNT2; -.
DR PRIDE; Q5SNT2; -.
DR ProteomicsDB; 63760; -. [Q5SNT2-1]
DR ProteomicsDB; 63761; -. [Q5SNT2-2]
DR Antibodypedia; 62878; 21 antibodies from 8 providers.
DR DNASU; 199953; -.
DR Ensembl; ENST00000340305.9; ENSP00000344772.5; ENSG00000188807.13. [Q5SNT2-2]
DR Ensembl; ENST00000340381.11; ENSP00000344503.6; ENSG00000188807.13. [Q5SNT2-1]
DR GeneID; 199953; -.
DR KEGG; hsa:199953; -.
DR MANE-Select; ENST00000340381.11; ENSP00000344503.6; NM_001130924.3; NP_001124396.2.
DR UCSC; uc001apy.4; human. [Q5SNT2-1]
DR CTD; 199953; -.
DR DisGeNET; 199953; -.
DR GeneCards; TMEM201; -.
DR HGNC; HGNC:33719; TMEM201.
DR HPA; ENSG00000188807; Tissue enhanced (skeletal).
DR neXtProt; NX_Q5SNT2; -.
DR OpenTargets; ENSG00000188807; -.
DR PharmGKB; PA162406359; -.
DR VEuPathDB; HostDB:ENSG00000188807; -.
DR eggNOG; KOG4623; Eukaryota.
DR GeneTree; ENSGT00390000002713; -.
DR HOGENOM; CLU_067578_0_0_1; -.
DR InParanoid; Q5SNT2; -.
DR OMA; LWFFILC; -.
DR OrthoDB; 532133at2759; -.
DR PhylomeDB; Q5SNT2; -.
DR TreeFam; TF106107; -.
DR PathwayCommons; Q5SNT2; -.
DR SignaLink; Q5SNT2; -.
DR BioGRID-ORCS; 199953; 26 hits in 1081 CRISPR screens.
DR ChiTaRS; TMEM201; human.
DR GenomeRNAi; 199953; -.
DR Pharos; Q5SNT2; Tbio.
DR PRO; PR:Q5SNT2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5SNT2; protein.
DR Bgee; ENSG00000188807; Expressed in cardiac muscle of right atrium and 156 other tissues.
DR ExpressionAtlas; Q5SNT2; baseline and differential.
DR Genevisible; Q5SNT2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IMP:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005521; F:lamin binding; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR GO; GO:0030473; P:nuclear migration along microtubule; IBA:GO_Central.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IDA:UniProtKB.
DR InterPro; IPR018617; Ima1_N.
DR InterPro; IPR040041; TMEM201.
DR InterPro; IPR018861; TMEM201_C.
DR PANTHER; PTHR28646; PTHR28646; 1.
DR Pfam; PF10476; DUF2448; 1.
DR Pfam; PF09779; Ima1_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..666
FT /note="Transmembrane protein 201"
FT /id="PRO_0000317198"
FT TOPO_DOM 1..213
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:21610090"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..297
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..322
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..356
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT TRANSMEM 357..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..644
FT /note="Nuclear"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:19494128"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT REGION 502..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 388..392
FT /note="FFPGD -> SEKQP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030915"
FT VAR_SEQ 393..666
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030916"
FT MUTAGEN 48
FT /note="C->A: Impairs organization of the nuclear envelope;
FT abolishes its localization to the nuclear envelope; impairs
FT localization of SUN1 and EMD to the nuclear envelope."
FT /evidence="ECO:0000269|PubMed:21610090"
FT MUTAGEN 121
FT /note="C->A: Abolishes localization to the nuclear
FT envelopee; abolishes its localization to the nuclear
FT envelope; impairs localization of SUN1 and EMD to the
FT nuclear envelope."
FT /evidence="ECO:0000269|PubMed:21610090"
SQ SEQUENCE 666 AA; 72236 MW; 19A4E0F866838525 CRC64;
MEGVSALLAR CPTAGLAGGL GVTACAAAGV LLYRIARRMK PTHTMVNCWF CNQDTLVPYG
NRNCWDCPHC EQYNGFQENG DYNKPIPAQY LEHLNHVVSS APSLRDPSQP QQWVSSQVLL
CKRCNHHQTT KIKQLAAFAP REEGRYDEEV EVYRHHLEQM YKLCRPCQAA VEYYIKHQNR
QLRALLLSHQ FKRREADQTH AQNFSSAVKS PVQVILLRAL AFLACAFLLT TALYGASGHF
APGTTVPLAL PPGGNGSATP DNGTTPGAEG WRQLLGLLPE HMAEKLCEAW AFGQSHQTGV
VALGLLTCLL AMLLAGRIRL RRIDAFCTCL WALLLGLHLA EQHLQAASPS WLDTLKFSTT
SLCCLVGFTA AVATRKATGP RRFRPRRFFP GDSAGLFPTS PSLAIPHPSV GGSPASLFIP
SPPSFLPLAN QQLFRSPRRT SPSSLPGRLS RALSLGTIPS LTRADSGYLF SGSRPPSQVS
RSGEFPVSDY FSLLSGSCPS SPLPSPAPSV AGSVASSSGS LRHRRPLISP ARLNLKGQKL
LLFPSPPGEA PTTPSSSDEH SPHNGSLFTM EPPHVPRKPP LQDVKHALDL RSKLERGSAC
SNRSIKKEDD SSQSSTCVVD TTTRGCSEEA ATWRGRFGPS LVRGLLAVSL AANALFTSVF
LYQSLR
