IGSF1_MOUSE
ID IGSF1_MOUSE Reviewed; 1317 AA.
AC Q7TQA1; Q6ZQD0; Q7TQ99; Q7TQA0; Q8BMN5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Immunoglobulin superfamily member 1;
DE Short=IgSF1;
DE AltName: Full=Inhibin-binding protein;
DE Short=InhBP;
DE Flags: Precursor;
GN Name=Igsf1; Synonyms=Kiaa0364;
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 [MRNA] (ISOFORMS 1; 3; 4 AND 5), AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Pituitary;
RX PubMed=12832474; DOI=10.1128/mcb.23.14.4882-4891.2003;
RA Bernard D.J., Burns K.H., Haupt B., Matzuk M.M., Woodruff T.K.;
RT "Normal reproductive function in InhBP/p120-deficient mice.";
RL Mol. Cell. Biol. 23:4882-4891(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23143598; DOI=10.1038/ng.2453;
RA Sun Y., Bak B., Schoenmakers N., van Trotsenburg A.S., Oostdijk W.,
RA Voshol P., Cambridge E., White J.K., le Tissier P., Gharavy S.N.,
RA Martinez-Barbera J.P., Stokvis-Brantsma W.H., Vulsma T., Kempers M.J.,
RA Persani L., Campi I., Bonomi M., Beck-Peccoz P., Zhu H., Davis T.M.,
RA Hokken-Koelega A.C., Del Blanco D.G., Rangasami J.J., Ruivenkamp C.A.,
RA Laros J.F., Kriek M., Kant S.G., Bosch C.A., Biermasz N.R.,
RA Appelman-Dijkstra N.M., Corssmit E.P., Hovens G.C., Pereira A.M.,
RA den Dunnen J.T., Wade M.G., Breuning M.H., Hennekam R.C., Chatterjee K.,
RA Dattani M.T., Wit J.M., Bernard D.J.;
RT "Loss-of-function mutations in IGSF1 cause an X-linked syndrome of central
RT hypothyroidism and testicular enlargement.";
RL Nat. Genet. 44:1375-1381(2012).
CC -!- FUNCTION: Seems to be a coreceptor in inhibin signaling, but seems not
CC to be a high-affinity inhibin receptor. Antagonizes activin A signaling
CC in the presence or absence of inhibin B. Necessary to mediate a
CC specific antagonistic effect of inhibin B on activin-stimulated
CC transcription (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with INHA; the interaction is not confirmed by
CC standard receptor binding assays (By similarity). Interacts with
CC ACVR1B; the interaction appears to be ligand-dependent as it is
CC diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B,
CC ACVRL1 and BMPR1B (By similarity). Interacts with HECTD1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=InhBP-L, long;
CC IsoId=Q7TQA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TQA1-2; Sequence=VSP_031203;
CC Name=3; Synonyms=InhBP-3;
CC IsoId=Q7TQA1-3; Sequence=VSP_031201, VSP_031202;
CC Name=4; Synonyms=InhBP-S, short;
CC IsoId=Q7TQA1-4; Sequence=VSP_031199, VSP_031200;
CC Name=5; Synonyms=InhBP-4, variant 4;
CC IsoId=Q7TQA1-5; Sequence=VSP_031198;
CC -!- DEVELOPMENTAL STAGE: Expressed at embryonic day (E) 12.5 in embryo.
CC {ECO:0000269|PubMed:23143598}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile and show no
CC alterations in FSH synthesis or secretion or in ovarian and testicular
CC function. According to PubMed:23143598 male mice show diminished
CC pituitary and serum thyroid-stimulating hormone (TSH) concentrations,
CC reduced pituitary thyrotropin-releasing hormone (TRH) receptor
CC expression, decreased triiodothyronine concentrations and increased
CC body mass. {ECO:0000269|PubMed:12832474, ECO:0000269|PubMed:23143598}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97936.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY227771; AAP57079.1; -; mRNA.
DR EMBL; AY227772; AAP57080.1; -; mRNA.
DR EMBL; AY227773; AAP57081.1; -; mRNA.
DR EMBL; AY227774; AAP57082.1; -; mRNA.
DR EMBL; AK129126; BAC97936.1; ALT_INIT; mRNA.
DR EMBL; AK030452; BAC26969.1; -; mRNA.
DR CCDS; CCDS40964.1; -. [Q7TQA1-1]
DR CCDS; CCDS40965.1; -. [Q7TQA1-5]
DR CCDS; CCDS40966.1; -. [Q7TQA1-3]
DR CCDS; CCDS40967.1; -. [Q7TQA1-4]
DR RefSeq; NP_808259.2; NM_177591.4. [Q7TQA1-1]
DR RefSeq; NP_808583.1; NM_177915.4. [Q7TQA1-4]
DR RefSeq; NP_899178.2; NM_183335.2. [Q7TQA1-3]
DR RefSeq; NP_899179.1; NM_183336.2. [Q7TQA1-5]
DR RefSeq; XP_006541550.1; XM_006541487.2. [Q7TQA1-3]
DR AlphaFoldDB; Q7TQA1; -.
DR SMR; Q7TQA1; -.
DR STRING; 10090.ENSMUSP00000033442; -.
DR GlyConnect; 2381; 1 N-Linked glycan (3 sites).
DR GlyGen; Q7TQA1; 8 sites, 1 N-linked glycan (3 sites).
DR iPTMnet; Q7TQA1; -.
DR PhosphoSitePlus; Q7TQA1; -.
DR PaxDb; Q7TQA1; -.
DR PRIDE; Q7TQA1; -.
DR ProteomicsDB; 267297; -. [Q7TQA1-1]
DR ProteomicsDB; 267298; -. [Q7TQA1-2]
DR ProteomicsDB; 267299; -. [Q7TQA1-3]
DR ProteomicsDB; 267301; -. [Q7TQA1-5]
DR Antibodypedia; 16308; 191 antibodies from 20 providers.
DR DNASU; 209268; -.
DR Ensembl; ENSMUST00000033442; ENSMUSP00000033442; ENSMUSG00000031111. [Q7TQA1-1]
DR Ensembl; ENSMUST00000072037; ENSMUSP00000071919; ENSMUSG00000031111. [Q7TQA1-3]
DR Ensembl; ENSMUST00000114891; ENSMUSP00000110541; ENSMUSG00000031111. [Q7TQA1-4]
DR Ensembl; ENSMUST00000114893; ENSMUSP00000110543; ENSMUSG00000031111. [Q7TQA1-5]
DR GeneID; 209268; -.
DR KEGG; mmu:209268; -.
DR UCSC; uc009tdg.2; mouse. [Q7TQA1-1]
DR UCSC; uc009tdi.1; mouse. [Q7TQA1-3]
DR UCSC; uc009tdj.2; mouse. [Q7TQA1-4]
DR CTD; 3547; -.
DR MGI; MGI:2147913; Igsf1.
DR VEuPathDB; HostDB:ENSMUSG00000031111; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_006143_0_0_1; -.
DR InParanoid; Q7TQA1; -.
DR OMA; GCGHGCW; -.
DR OrthoDB; 1327293at2759; -.
DR PhylomeDB; Q7TQA1; -.
DR TreeFam; TF336644; -.
DR BioGRID-ORCS; 209268; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Igsf1; mouse.
DR PRO; PR:Q7TQA1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q7TQA1; protein.
DR Bgee; ENSMUSG00000031111; Expressed in arcuate nucleus of hypothalamus and 131 other tissues.
DR Genevisible; Q7TQA1; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0038102; F:activin receptor antagonist activity; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; ISO:MGI.
DR GO; GO:0034711; F:inhibin binding; ISO:MGI.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 12.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 4.
DR SMART; SM00409; IG; 11.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 12.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1317
FT /note="Immunoglobulin superfamily member 1"
FT /id="PRO_0000318513"
FT TOPO_DOM 21..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..1317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 21..112
FT /note="Ig-like C2-type 1"
FT DOMAIN 114..211
FT /note="Ig-like C2-type 2"
FT DOMAIN 216..302
FT /note="Ig-like C2-type 3"
FT DOMAIN 311..398
FT /note="Ig-like C2-type 4"
FT DOMAIN 400..481
FT /note="Ig-like C2-type 5"
FT DOMAIN 570..658
FT /note="Ig-like C2-type 6"
FT DOMAIN 659..753
FT /note="Ig-like C2-type 7"
FT DOMAIN 758..850
FT /note="Ig-like C2-type 8"
FT DOMAIN 854..938
FT /note="Ig-like C2-type 9"
FT DOMAIN 946..1041
FT /note="Ig-like C2-type 10"
FT DOMAIN 1046..1131
FT /note="Ig-like C2-type 11"
FT DOMAIN 1142..1223
FT /note="Ig-like C2-type 12"
FT REGION 1290..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 238..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 333..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 422..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 780..830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 876..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1068..1115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1164..1207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..542
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12832474"
FT /id="VSP_031198"
FT VAR_SEQ 214..232
FT /note="LYPKPTLTAHPGPILAPGE -> GCGHGCWHLTIVIPGIMAG (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12832474,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031199"
FT VAR_SEQ 233..1317
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12832474,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031200"
FT VAR_SEQ 755..762
FT /note="EMYPKPFF -> DGRTKAQN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12832474"
FT /id="VSP_031201"
FT VAR_SEQ 763..1317
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12832474"
FT /id="VSP_031202"
FT VAR_SEQ 865..1156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_031203"
FT CONFLICT 277
FT /note="K -> E (in Ref. 1; AAP57081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1317 AA; 147010 MW; 09D1E7A89ADCB04D CRC64;
MMLRTFTLLL LCIWLNPGMT SLAVESQPEL WIESNYPQAP WENITLWCKS PSRVSSKFLL
LKDNSQMTWI RPPYKTFQVS FFIGALTESN TGLYRCCYWK EKGWSKPSKI LELEAPGQLP
KPIFWIQAET PPLPGCNVNI FCHGWLQDLV FMLFKEGYTE PVDYQVPTGT MAIFSIDNLA
PENEGVYICR THIQMLPTLW SEPSNPLKLV VAGLYPKPTL TAHPGPILAP GESLSLRCQG
PIYGMTFALM RLEDLKKSFY HKKPIKNEAY FYFQDLKIQD TGHYLCFYYD GSYRGSLLSD
ILKIWVTDTF PKTWLLVQPS PVIQMGQNVS LRCGGLMDGV GLALYKKGEE KPLQFLDASS
NTGNNSFFLK NVTYRDAGIY SCHYYLTWKT SIKMATYNTV ELMVVAWPSS VFKVGKTITL
QCRVSHPVLE FSLEWEERTT FQKFSVDGDF LITDIEGQGT GTYSCSYRIE AHPNTWSHRS
KPLKLVGPAG FLTWNSILNE AVRVSLTMQL ASLLLLVVWI RWKCRRLRLR EAWLLGTAQG
VAMLFILMAL LCCGLCNGAL TEEIEIVMPT PKPELWAETN FPLAPWKNLT LWCRSPSGST
KEFVLLKDGT GWIATRPASE QVRAAFPLGA LTHSHTGSYH CHSWEEMAVS EPSEALELVG
TDILPKPVIS ASLPIRGQEL QIRCKGWLEG LGFALYKKGE QEPVQQLGAV GREAFFTIQR
MEDKDEGNYS CRTHTEMQPF KWSEPSEPLE LVIKEMYPKP FFKTWASPVV TPGSRVTFNC
STSHEHMSFI LYKDGNEIAS SDLAWGNPGG STAHFLIISV GIGDGGNYSC RYYDFSIWSE
PSNPVELVVT EFYPKPTLLA QPGPVVLPGK NVTLRCQGIF QGMRFALLQE GTHTPLQFQS
TSGTSADFLL HTVGAQDFGN YSCVYYETTM SNRGSSLSTP LMIWVTDTFP RPWLSAEPSS
VVTMGQNVTL WCQGPVRGVG YILHKEGEAT SMQLWGSTSN EGAFPIINIS GASIGRYSCC
YHPDWMSPIK IQPSNTLELI VTGLLPKPSL LVQPGPMVAP GENVTLQCQG ELPDSTFVLL
KEGTRQPLEQ QRPSGYRADF WMPVVRDQDS GVYSCVYYLD SAPLVASNHS NSLEIWVTDK
PPKPSLSAWP STIFKLGKDI TLQCRGPLPG VEFVLEHDGE EAPQQFSEDG DFVIDNLEGK
GIGNYSCSYR LQAYPDIWSE PSDTLELVGA AGPVAQECTV GNIVRSTLIV VVVVALGIVL
AVEWKKWPRL RTRGSETDGR DQTVVLEECN QEGEPGTTTN SPSSASQEVS VELTVPI
