IGS10_HUMAN
ID IGS10_HUMAN Reviewed; 2623 AA.
AC Q6WRI0; Q86YJ9; Q8N772; Q8NA84;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Immunoglobulin superfamily member 10;
DE Short=IgSF10;
DE AltName: Full=Calvaria mechanical force protein 608;
DE Short=CMF608;
DE Flags: Precursor;
GN Name=IGSF10; Synonyms=CMF608;
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 1).
RX PubMed=14962803; DOI=10.1016/j.bone.2003.10.003;
RA Segev O., Samach A., Faerman A., Kalinski H., Beiman M., Gelfand A.,
RA Turam H., Boguslavsky S., Moshayov A., Gottlieb H., Kazanov E., Nevo Z.,
RA Robinson D., Skaliter R., Einat P., Binderman I., Feinstein E.;
RT "CMF608 -- a novel mechanical strain-induced bone-specific protein
RT expressed in early osteochondroprogenitor cells.";
RL Bone 34:246-260(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2187-2623 (ISOFORM 1).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 SUBCELLULAR LOCATION, PROBABLE INVOLVEMENT IN SELF-LIMITED DELAYED PUBERTY,
RP VARIANTS LEU-156; LYS-161; GLY-2264 AND ASN-2614, AND CHARACTERIZATION OF
RP VARIANTS LEU-156 AND LYS-161.
RX PubMed=27137492; DOI=10.15252/emmm.201606250;
RA Howard S.R., Guasti L., Ruiz-Babot G., Mancini A., David A., Storr H.L.,
RA Metherell L.A., Sternberg M.J., Cabrera C.P., Warren H.R., Barnes M.R.,
RA Quinton R., de Roux N., Young J., Guiochon-Mantel A., Wehkalampi K.,
RA Andre V., Gothilf Y., Cariboni A., Dunkel L.;
RT "IGSF10 mutations dysregulate gonadotropin-releasing hormone neuronal
RT migration resulting in delayed puberty.";
RL EMBO Mol. Med. 8:626-642(2016).
CC -!- FUNCTION: Involved in the control of early migration of neurons
CC expressing gonadotropin-releasing hormone (GNRH neurons) (By
CC similarity). May be involved in the maintenance of
CC osteochondroprogenitor cells pool (By similarity).
CC {ECO:0000250|UniProtKB:Q3V1M1, ECO:0000250|UniProtKB:Q6WRH9}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27137492}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6WRI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6WRI0-2; Sequence=VSP_025195, VSP_025196;
CC Name=3;
CC IsoId=Q6WRI0-3; Sequence=VSP_025194;
CC -!- DISEASE: Note=Mutations in IGSF10 may be a cause of self-limited
CC delayed puberty. This common condition is defined as the absence of
CC testicular enlargement in boys or breast development in girls at an age
CC that is 2-2.5 standard deviations later than the population mean. Self-
CC limited delayed puberty segregates within families, with the majority
CC of families displaying an autosomal dominant pattern of inheritance.
CC {ECO:0000269|PubMed:27137492}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05429.1; Type=Erroneous initiation; 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; AY273815; AAQ16156.1; -; mRNA.
DR EMBL; AK093069; BAC04042.1; -; mRNA.
DR EMBL; AK098838; BAC05429.1; ALT_INIT; mRNA.
DR EMBL; BC031063; AAH31063.1; -; mRNA.
DR CCDS; CCDS3160.1; -. [Q6WRI0-1]
DR RefSeq; NP_001171616.1; NM_001178145.1. [Q6WRI0-3]
DR RefSeq; NP_001171617.1; NM_001178146.1. [Q6WRI0-3]
DR RefSeq; NP_849144.2; NM_178822.4. [Q6WRI0-1]
DR RefSeq; XP_011511011.1; XM_011512709.2. [Q6WRI0-1]
DR AlphaFoldDB; Q6WRI0; -.
DR SMR; Q6WRI0; -.
DR BioGRID; 130074; 6.
DR IntAct; Q6WRI0; 1.
DR STRING; 9606.ENSP00000282466; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR CarbonylDB; Q6WRI0; -.
DR GlyGen; Q6WRI0; 11 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q6WRI0; -.
DR PhosphoSitePlus; Q6WRI0; -.
DR BioMuta; IGSF10; -.
DR DMDM; 74749492; -.
DR EPD; Q6WRI0; -.
DR jPOST; Q6WRI0; -.
DR MassIVE; Q6WRI0; -.
DR PaxDb; Q6WRI0; -.
DR PeptideAtlas; Q6WRI0; -.
DR PRIDE; Q6WRI0; -.
DR ProteomicsDB; 67774; -. [Q6WRI0-1]
DR ProteomicsDB; 67775; -. [Q6WRI0-2]
DR ProteomicsDB; 67776; -. [Q6WRI0-3]
DR Antibodypedia; 2541; 66 antibodies from 14 providers.
DR DNASU; 285313; -.
DR Ensembl; ENST00000282466.4; ENSP00000282466.3; ENSG00000152580.9. [Q6WRI0-1]
DR GeneID; 285313; -.
DR KEGG; hsa:285313; -.
DR MANE-Select; ENST00000282466.4; ENSP00000282466.3; NM_178822.5; NP_849144.2.
DR UCSC; uc011bod.3; human. [Q6WRI0-1]
DR CTD; 285313; -.
DR DisGeNET; 285313; -.
DR GeneCards; IGSF10; -.
DR HGNC; HGNC:26384; IGSF10.
DR HPA; ENSG00000152580; Tissue enhanced (ovary).
DR MIM; 617351; gene.
DR neXtProt; NX_Q6WRI0; -.
DR OpenTargets; ENSG00000152580; -.
DR PharmGKB; PA134900760; -.
DR VEuPathDB; HostDB:ENSG00000152580; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158290; -.
DR HOGENOM; CLU_000580_0_0_1; -.
DR InParanoid; Q6WRI0; -.
DR OMA; IWGRGRI; -.
DR OrthoDB; 8971at2759; -.
DR PhylomeDB; Q6WRI0; -.
DR TreeFam; TF326318; -.
DR PathwayCommons; Q6WRI0; -.
DR SignaLink; Q6WRI0; -.
DR BioGRID-ORCS; 285313; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; IGSF10; human.
DR GenomeRNAi; 285313; -.
DR Pharos; Q6WRI0; Tbio.
DR PRO; PR:Q6WRI0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6WRI0; protein.
DR Bgee; ENSG00000152580; Expressed in cardiac muscle of right atrium and 153 other tissues.
DR ExpressionAtlas; Q6WRI0; baseline and differential.
DR Genevisible; Q6WRI0; HS.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 12.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF07679; I-set; 7.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 12.
DR SMART; SM00408; IGc2; 12.
DR SMART; SM00406; IGv; 7.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 12.
DR PROSITE; PS50835; IG_LIKE; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Osteogenesis; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..2623
FT /note="Immunoglobulin superfamily member 10"
FT /id="PRO_0000286817"
FT DOMAIN 29..56
FT /note="LRRNT"
FT REPEAT 58..79
FT /note="LRR 1"
FT REPEAT 82..103
FT /note="LRR 2"
FT REPEAT 106..127
FT /note="LRR 3"
FT REPEAT 130..151
FT /note="LRR 4"
FT REPEAT 154..175
FT /note="LRR 5"
FT REPEAT 186..207
FT /note="LRR 6"
FT DOMAIN 219..281
FT /note="LRRCT"
FT DOMAIN 461..567
FT /note="Ig-like C2-type 1"
FT DOMAIN 571..661
FT /note="Ig-like C2-type 2"
FT DOMAIN 1648..1739
FT /note="Ig-like C2-type 3"
FT DOMAIN 1745..1836
FT /note="Ig-like C2-type 4"
FT DOMAIN 1841..1933
FT /note="Ig-like C2-type 5"
FT DOMAIN 1941..2034
FT /note="Ig-like C2-type 6"
FT DOMAIN 2037..2135
FT /note="Ig-like C2-type 7"
FT DOMAIN 2141..2229
FT /note="Ig-like C2-type 8"
FT DOMAIN 2234..2331
FT /note="Ig-like C2-type 9"
FT DOMAIN 2337..2427
FT /note="Ig-like C2-type 10"
FT DOMAIN 2432..2518
FT /note="Ig-like C2-type 11"
FT DOMAIN 2528..2623
FT /note="Ig-like C2-type 12"
FT REGION 668..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2603
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6WRH9"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1962
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 497..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 595..645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1670..1723
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1767..1820
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1864..1917
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1963..2016
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2060..2119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2163..2213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2261..2313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2359..2411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2454..2506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2550..2605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..2021
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025194"
FT VAR_SEQ 1..1973
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025195"
FT VAR_SEQ 1974..1987
FT /note="MWRLPSKAVVDQQH -> MVESVRLENQPCDL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025196"
FT VARIANT 124
FT /note="T -> I (in dbSNP:rs35953658)"
FT /id="VAR_032179"
FT VARIANT 150
FT /note="Y -> D (in dbSNP:rs7619322)"
FT /id="VAR_032180"
FT VARIANT 156
FT /note="R -> L (probable disease-associated variant found in
FT autosomal dominant self-limited delayed puberty; the mutant
FT protein is not secreted; dbSNP:rs138756085)"
FT /evidence="ECO:0000269|PubMed:27137492"
FT /id="VAR_078550"
FT VARIANT 161
FT /note="E -> K (probable disease-associated variant found in
FT autosomal dominant self-limited delayed puberty; the mutant
FT protein is not secreted; dbSNP:rs114161831)"
FT /evidence="ECO:0000269|PubMed:27137492"
FT /id="VAR_078551"
FT VARIANT 571
FT /note="P -> S (in dbSNP:rs17204557)"
FT /id="VAR_032181"
FT VARIANT 795
FT /note="D -> N (in dbSNP:rs58583961)"
FT /id="VAR_061313"
FT VARIANT 1199
FT /note="S -> A (in dbSNP:rs16863403)"
FT /id="VAR_032182"
FT VARIANT 1370
FT /note="T -> I (in dbSNP:rs34933248)"
FT /id="VAR_032183"
FT VARIANT 1875
FT /note="Y -> H (in dbSNP:rs12487205)"
FT /id="VAR_032184"
FT VARIANT 2264
FT /note="E -> G (found in autosomal dominant self-limited
FT delayed puberty; unknown pathological significance;
FT dbSNP:rs1204847665)"
FT /evidence="ECO:0000269|PubMed:27137492"
FT /id="VAR_078552"
FT VARIANT 2476
FT /note="R -> W (in dbSNP:rs3732775)"
FT /id="VAR_032185"
FT VARIANT 2579
FT /note="H -> Y (in dbSNP:rs7624011)"
FT /id="VAR_032186"
FT VARIANT 2614
FT /note="D -> N (found in autosomal dominant self-limited
FT delayed puberty; unknown pathological significance;
FT dbSNP:rs112889898)"
FT /evidence="ECO:0000269|PubMed:27137492"
FT /id="VAR_078553"
FT CONFLICT 2243
FT /note="N -> S (in Ref. 3; AAH31063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2623 AA; 290838 MW; CBE7139B0DF16CF8 CRC64;
MKVKGRGITC LLVSFAVICL VATPGGKACP RRCACYMPTE VHCTFRYLTS IPDSIPPNVE
RINLGYNSLV RLMETDFSGL TKLELLMLHS NGIHTIPDKT FSDLQALQVL KMSYNKVRKL
QKDTFYGLRS LTRLHMDHNN IEFINPEVFY GLNFLRLVHL EGNQLTKLHP DTFVSLSYLQ
IFKISFIKFL YLSDNFLTSL PQEMVSYMPD LDSLYLHGNP WTCDCHLKWL SDWIQEKPDV
IKCKKDRSPS SAQQCPLCMN PRTSKGKPLA MVSAAAFQCA KPTIDSSLKS KSLTILEDSS
SAFISPQGFM APFGSLTLNM TDQSGNEANM VCSIQKPSRT SPIAFTEEND YIVLNTSFST
FLVCNIDYGH IQPVWQILAL YSDSPLILER SHLLSETPQL YYKYKQVAPK PEDIFTNIEA
DLRADPSWLM QDQISLQLNR TATTFSTLQI QYSSDAQITL PRAEMRPVKH KWTMISRDNN
TKLEHTVLVG GTVGLNCPGQ GDPTPHVDWL LADGSKVRAP YVSEDGRILI DKSGKLELQM
ADSFDTGVYH CISSNYDDAD ILTYRITVVE PLVEAYQENG IHHTVFIGET LDLPCHSTGI
PDASISWVIP GNNVLYQSSR DKKVLNNGTL RILQVTPKDQ GYYRCVAANP SGVDFLIFQV
SVKMKGQRPL EHDGETEGSG LDESNPIAHL KEPPGAQLRT SALMEAEVGK HTSSTSKRHN
YRELTLQRRG DSTHRRFREN RRHFPPSARR IDPQHWAALL EKAKKNAMPD KRENTTVSPP
PVVTQLPNIP GEEDDSSGML ALHEEFMVPA TKALNLPART VTADSRTISD SPMTNINYGT
EFSPVVNSQI LPPEEPTDFK LSTAIKTTAM SKNINPTMSS QIQGTTNQHS STVFPLLLGA
TEFQDSDQMG RGREHFQSRP PITVRTMIKD VNVKMLSSTT NKLLLESVNT TNSHQTSVRE
VSEPRHNHFY SHTTQILSTS TFPSDPHTAA HSQFPIPRNS TVNIPLFRRF GRQRKIGGRG
RIISPYRTPV LRRHRYSIFR STTRGSSEKS TTAFSATVLN VTCLSCLPRE RLTTATAALS
FPSAAPITFP KADIARVPSE ESTTLVQNPL LLLENKPSVE KTTPTIKYFR TEISQVTPTG
AVMTYAPTSI PMEKTHKVNA SYPRVSSTNE AKRDSVITSS LSGAITKPPM TIIAITRFSR
RKIPWQQNFV NNHNPKGRLR NQHKVSLQKS TAVMLPKTSP ALPRDKVSPF HFTTLSTSVM
QIPSNTLTTA HHTTTKTHNP GSLPTKKELP FPPLNPMLPS IISKDSSTKS IISTQTAIPA
TTPTFPASVI TYETQTERSR AQTIQREQEP QKKNRTDPNI SPDQSSGFTT PTAMTPPVLT
TAETSVKPSV SAFTHSPPEN TTGISSTISF HSRTLNLTDV IEELAQASTQ TLKSTIASET
TLSSKSHQST TTRKAIIRHS TIPPFLSSSA TLMPVPISPP FTQRAVTDNV ATPISGLMTN
TVVKLHESSR HNAKPQQLVA EVATSPKVHP NAKFTIGTTH FIYSNLLHST PMPALTTVKS
QNSKLTPSPW AENQFWHKPY SEIAEKGKKP EVSMLATTGL SEATTLVSDW DGQKNTKKSD
FDKKPVQEAT TSKLLPFDSL SRYIFEKPRI VGGKAASFTI PANSDAFLPC EAVGNPLPTI
HWTRVPSGLD LSKRKQNSRV QVLPNGTLSI QRVEIQDRGQ YLCSASNLFG TDHLHVTLSV
VSYPPRILER RTKEITVHSG STVELKCRAE GRPSPTVTWI LANQTVVSES SQGSRQAVVT
VDGTLVLHNL SIYDRGFYKC VASNPGGQDS LLVKIQVIAA PPVILEQRRQ VIVGTWGESL
KLPCTAKGTP QPSVYWVLSD GTEVKPLQFT NSKLFLFSNG TLYIRNLASS DRGTYECIAT
SSTGSERRVV MLTMEERVTS PRIEAASQKR TEVNFGDKLL LNCSATGEPK PQIMWRLPSK
AVVDQQHRVG SWIHVYPNGS LFIGSVTEKD SGVYLCVARN KMGDDLILMH VSLRLKPAKI
DHKQYFRKQV LHGKDFQVDC KASGSPVPEI SWSLPDGTMI NNAMQADDSG HRTRRYTLFN
NGTLYFNKVG VAEEGDYTCY AQNTLGKDEM KVHLTVITAA PRIRQSNKTN KRIKAGDTAV
LDCEVTGDPK PKIFWLLPSN DMISFSIDRY TFHANGSLTI NKVKLLDSGE YVCVARNPSG
DDTKMYKLDV VSKPPLINGL YTNRTVIKAT AVRHSKKHFD CRAEGTPSPE VMWIMPDNIF
LTAPYYGSRI TVHKNGTLEI RNVRLSDSAD FICVARNEGG ESVLVVQLEV LEMLRRPTFR
NPFNEKIVAQ LGKSTALNCS VDGNPPPEII WILPNGTRFS NGPQSYQYLI ASNGSFIISK
TTREDAGKYR CAARNKVGYI EKLVILEIGQ KPVILTYAPG TVKGISGESL SLHCVSDGIP
KPNIKWTMPS GYVVDRPQIN GKYILHDNGT LVIKEATAYD RGNYICKAQN SVGHTLITVP
VMIVAYPPRI TNRPPRSIVT RTGAAFQLHC VALGVPKPEI TWEMPDHSLL STASKERTHG
SEQLHLQGTL VIQNPQTSDS GIYKCTAKNP LGSDYAATYI QVI