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 27-MAR-2024, entry version 159. 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; 7. DR IntAct; Q6WRI0; 1. DR STRING; 9606.ENSP00000282466; -. DR DrugBank; DB00114; Pyridoxal phosphate. DR CarbonylDB; Q6WRI0; -. DR GlyCosmos; Q6WRI0; 10 sites, 1 glycan. DR GlyGen; Q6WRI0; 13 sites, 3 O-linked glycans (5 sites). DR iPTMnet; Q6WRI0; -. DR PhosphoSitePlus; Q6WRI0; -. DR BioMuta; IGSF10; -. DR DMDM; 74749492; -. DR EPD; Q6WRI0; -. DR jPOST; Q6WRI0; -. DR MassIVE; Q6WRI0; -. DR PaxDb; 9606-ENSP00000282466; -. DR PeptideAtlas; Q6WRI0; -. DR ProteomicsDB; 67774; -. [Q6WRI0-1] DR ProteomicsDB; 67775; -. [Q6WRI0-2] DR ProteomicsDB; 67776; -. [Q6WRI0-3] DR Pumba; Q6WRI0; -. DR Antibodypedia; 2541; 85 antibodies from 15 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 AGR; HGNC:26384; -. DR CTD; 285313; -. DR DisGeNET; 285313; -. DR GeneCards; IGSF10; -. DR HGNC; HGNC:26384; IGSF10. DR HPA; ENSG00000152580; Tissue enhanced (gallbladder, 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; VTWIMPD; -. DR OrthoDB; 2918193at2759; -. DR PhylomeDB; Q6WRI0; -. DR TreeFam; TF326318; -. DR PathwayCommons; Q6WRI0; -. DR SignaLink; Q6WRI0; -. DR BioGRID-ORCS; 285313; 7 hits in 1143 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 155 other cell types or tissues. DR ExpressionAtlas; Q6WRI0; baseline and differential. 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 CDD; cd00096; Ig; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 12. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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 PANTHER; PTHR45842:SF2; IMMUNOGLOBULIN SUPERFAMILY MEMBER 10; 1. DR PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1. DR Pfam; PF07679; I-set; 5. DR Pfam; PF13927; Ig_3; 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; Immunoglobulin; 12. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS50835; IG_LIKE; 12. DR Genevisible; Q6WRI0; HS. 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 (found in autosomal dominant self-limited FT delayed puberty; likely pathogenic; the mutant protein is FT not secreted; dbSNP:rs138756085)" FT /evidence="ECO:0000269|PubMed:27137492" FT /id="VAR_078550" FT VARIANT 161 FT /note="E -> K (found in autosomal dominant self-limited FT delayed puberty; likely pathogenic; the mutant protein is FT 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; uncertain 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; uncertain 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 //