RIN3_HUMAN
ID RIN3_HUMAN Reviewed; 985 AA.
AC Q8TB24; Q76LB3; Q8NF30; Q8TEE8; Q8WYP4; Q9H6A5; Q9HAG1;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ras and Rab interactor 3;
DE AltName: Full=Ras interaction/interference protein 3;
GN Name=RIN3;
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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH BIN1 AND
RP RAB5B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12972505; DOI=10.1242/jcs.00718;
RA Kajiho H., Saito K., Tsujita K., Kontani K., Araki Y., Kurosu H.,
RA Katada T.;
RT "RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the
RT early endocytic pathway.";
RL J. Cell Sci. 116:4159-4168(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167 AND 405-985 (ISOFORM 1),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-985 (ISOFORM 4), AND VARIANT
RP MET-425.
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-985 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 435-959 (ISOFORM 1).
RC TISSUE=Leukocyte, and Spleen;
RX PubMed=11733506; DOI=10.1074/jbc.m106276200;
RA Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.;
RT "A novel binding protein composed of homophilic tetramer exhibits unique
RT properties for the small GTPase Rab5.";
RL J. Biol. Chem. 277:3412-3418(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=18486601; DOI=10.1016/j.bbrc.2008.05.027;
RA Yoshikawa M., Kajiho H., Sakurai K., Minoda T., Nakagawa S., Kontani K.,
RA Katada T.;
RT "Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF,
RT to early endocytic vesicles.";
RL Biochem. Biophys. Res. Commun. 372:168-172(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-825 AND THR-828, AND
RP INTERACTION WITH RAB31.
RX PubMed=21586568; DOI=10.1074/jbc.m110.172445;
RA Kajiho H., Sakurai K., Minoda T., Yoshikawa M., Nakagawa S., Fukushima S.,
RA Kontani K., Katada T.;
RT "Characterization of RIN3 as a guanine nucleotide exchange factor for the
RT Rab5 subfamily GTPase Rab31.";
RL J. Biol. Chem. 286:24364-24373(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 452-467 IN COMPLEX WITH CD2AP,
RP AND INTERACTION WITH CD2AP.
RG Structural genomics consortium (SGC);
RT "Atomic resolution crystal structure of the 2nd SH3 domain from human CD2AP
RT (CMS) in complex with a proline-rich peptide from human RIN3.";
RL Submitted (DEC-2011) to the PDB data bank.
CC -!- FUNCTION: Ras effector protein that functions as a guanine nucleotide
CC exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free
CC GTP. Required for normal RAB31 function. {ECO:0000269|PubMed:12972505,
CC ECO:0000269|PubMed:21586568}.
CC -!- SUBUNIT: Interacts with CD2AP, RAB5B, RAB31 and BIN1.
CC {ECO:0000269|PubMed:12972505, ECO:0000269|PubMed:21586568,
CC ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC Q8TB24; O00499: BIN1; NbExp=2; IntAct=EBI-1570523, EBI-719094;
CC Q8TB24; Q9Y5K6: CD2AP; NbExp=3; IntAct=EBI-1570523, EBI-298152;
CC Q8TB24; P46108: CRK; NbExp=2; IntAct=EBI-1570523, EBI-886;
CC Q8TB24; P16333: NCK1; NbExp=2; IntAct=EBI-1570523, EBI-389883;
CC Q8TB24; P19174: PLCG1; NbExp=3; IntAct=EBI-1570523, EBI-79387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18486601,
CC ECO:0000269|PubMed:21586568}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:12972505, ECO:0000269|PubMed:18486601,
CC ECO:0000269|PubMed:21586568}. Early endosome
CC {ECO:0000269|PubMed:18486601}. Note=Activation of tyrosine
CC phosphorylation signaling induces translocation to cytoplasmic
CC vesicles. {ECO:0000269|PubMed:18486601}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TB24-1; Sequence=Displayed;
CC Name=4;
CC IsoId=Q8TB24-4; Sequence=VSP_007587, VSP_007588;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12972505}.
CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13888.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAB15357.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03432.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB081753; BAC16513.1; -; mRNA.
DR EMBL; AL136332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK021762; BAB13888.1; ALT_SEQ; mRNA.
DR EMBL; AK026092; BAB15357.1; ALT_INIT; mRNA.
DR EMBL; AK074176; BAB85002.1; -; mRNA.
DR EMBL; AK090451; BAC03432.1; ALT_SEQ; mRNA.
DR EMBL; BC025248; AAH25248.2; -; mRNA.
DR EMBL; AB060338; BAB84316.1; -; mRNA.
DR CCDS; CCDS32144.1; -. [Q8TB24-1]
DR PIR; T50623; T50623.
DR RefSeq; NP_001306916.1; NM_001319987.1.
DR RefSeq; NP_079108.3; NM_024832.4. [Q8TB24-1]
DR PDB; 3U23; X-ray; 1.11 A; B=452-467.
DR PDB; 4WCI; X-ray; 1.65 A; B/D/F=378-393.
DR PDBsum; 3U23; -.
DR PDBsum; 4WCI; -.
DR AlphaFoldDB; Q8TB24; -.
DR SMR; Q8TB24; -.
DR BioGRID; 122974; 458.
DR IntAct; Q8TB24; 419.
DR MINT; Q8TB24; -.
DR STRING; 9606.ENSP00000216487; -.
DR MoonDB; Q8TB24; Predicted.
DR iPTMnet; Q8TB24; -.
DR PhosphoSitePlus; Q8TB24; -.
DR BioMuta; RIN3; -.
DR DMDM; 209572780; -.
DR EPD; Q8TB24; -.
DR jPOST; Q8TB24; -.
DR MassIVE; Q8TB24; -.
DR PaxDb; Q8TB24; -.
DR PeptideAtlas; Q8TB24; -.
DR PRIDE; Q8TB24; -.
DR ProteomicsDB; 73951; -. [Q8TB24-1]
DR ProteomicsDB; 73952; -. [Q8TB24-4]
DR Antibodypedia; 26773; 89 antibodies from 23 providers.
DR DNASU; 79890; -.
DR Ensembl; ENST00000216487.12; ENSP00000216487.7; ENSG00000100599.16. [Q8TB24-1]
DR GeneID; 79890; -.
DR KEGG; hsa:79890; -.
DR MANE-Select; ENST00000216487.12; ENSP00000216487.7; NM_024832.5; NP_079108.3.
DR UCSC; uc001yap.4; human. [Q8TB24-1]
DR CTD; 79890; -.
DR DisGeNET; 79890; -.
DR GeneCards; RIN3; -.
DR HGNC; HGNC:18751; RIN3.
DR HPA; ENSG00000100599; Tissue enhanced (bone).
DR MIM; 610223; gene.
DR neXtProt; NX_Q8TB24; -.
DR NIAGADS; ENSG00000100599; -.
DR OpenTargets; ENSG00000100599; -.
DR PharmGKB; PA38673; -.
DR VEuPathDB; HostDB:ENSG00000100599; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000158622; -.
DR InParanoid; Q8TB24; -.
DR OMA; YCFVYHP; -.
DR PhylomeDB; Q8TB24; -.
DR TreeFam; TF331067; -.
DR PathwayCommons; Q8TB24; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q8TB24; -.
DR BioGRID-ORCS; 79890; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; RIN3; human.
DR GenomeRNAi; 79890; -.
DR Pharos; Q8TB24; Tbio.
DR PRO; PR:Q8TB24; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8TB24; protein.
DR Bgee; ENSG00000100599; Expressed in granulocyte and 133 other tissues.
DR ExpressionAtlas; Q8TB24; baseline and differential.
DR Genevisible; Q8TB24; HS.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0031982; C:vesicle; IDA:ARUK-UCL.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0060755; P:negative regulation of mast cell chemotaxis; IMP:ARUK-UCL.
DR GO; GO:0002091; P:negative regulation of receptor internalization; IMP:ARUK-UCL.
DR GO; GO:0097494; P:regulation of vesicle size; IDA:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd10395; SH2_RIN3; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR035869; RIN3_SH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; GTPase activation; Reference proteome; SH2 domain.
FT CHAIN 1..985
FT /note="Ras and Rab interactor 3"
FT /id="PRO_0000191322"
FT DOMAIN 63..158
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 703..846
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT DOMAIN 877..963
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..732
FT /note="Interaction with RAB5B"
FT /evidence="ECO:0000269|PubMed:12972505"
FT COMPBIAS 275..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 878..903
FT /note="DFICVSYLEPEQQARTLASRADTQAQ -> VRPESGRGPVGPCPRHHPCCLL
FT AKEP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007587"
FT VAR_SEQ 904..985
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007588"
FT VARIANT 111
FT /note="E -> K (in dbSNP:rs2274542)"
FT /id="VAR_046645"
FT VARIANT 215
FT /note="H -> L (in dbSNP:rs3829947)"
FT /id="VAR_059960"
FT VARIANT 215
FT /note="H -> P (in dbSNP:rs3829947)"
FT /id="VAR_046646"
FT VARIANT 215
FT /note="H -> R (in dbSNP:rs3829947)"
FT /id="VAR_059961"
FT VARIANT 425
FT /note="T -> I (in dbSNP:rs3742717)"
FT /id="VAR_052946"
FT VARIANT 425
FT /note="T -> M (in dbSNP:rs3742717)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_046647"
FT VARIANT 613
FT /note="G -> A (in dbSNP:rs12434929)"
FT /id="VAR_046648"
FT MUTAGEN 825
FT /note="Y->A: Strongly reduced guanine nucleotide exchange
FT factor activity toward RAB31; when associated with A-828."
FT /evidence="ECO:0000269|PubMed:21586568"
FT MUTAGEN 828
FT /note="T->A: Strongly reduced guanine nucleotide exchange
FT factor activity toward RAB31; when associated with A-825."
FT /evidence="ECO:0000269|PubMed:21586568"
FT CONFLICT 742
FT /note="I -> F (in Ref. 4; AAH25248)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="Missing (in Ref. 3; BAB15357 and 4; AAH25248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 985 AA; 107854 MW; A8949EA0D61570BB CRC64;
MIRHAGAPAR GDPTGPVPVV GKGEEEEEED GMRLCLPANP KNCLPHRRGI SILEKLIKTC
PVWLQLSLGQ AEVARILHRV VAGMFLVRRD SSSKQLVLCV HFPSLNESSA EVLEYTIKEE
KSILYLEGSA LVFEDIFRLI AFYCVSRDLL PFTLRLPQAI LEASSFTDLE TIANLGLGFW
DSSLNPPQER GKPAEPPRDR APGFPLVSSL RPTAHDANCA CEIELSVGND RLWFVNPIFI
EDCSSALPTD QPPLGNCPAR PLPPTSDATS PTSRWAPRRP PPPPPVLPLQ PCSPAQPPVL
PALAPAPACP LPTSPPVPAP HVTPHAPGPP DHPNQPPMMT CERLPCPTAG LGPLREEAMK
PGAASSPLQQ VPAPPLPAKK NLPTAPPRRR VSERVSLEDQ SPGMAAEGDQ LSLPPQGTSD
GPEDTPREST EQGQDTEVKA SDPHSMPELP RTAKQPPVPP PRKKRISRQL ASTLPAPLEN
AELCTQAMAL ETPTPGPPRE GQSPASQAGT QHPPAQATAH SQSSPEFKGS LASLSDSLGV
SVMATDQDSY STSSTEEELE QFSSPSVKKK PSMILGKARH RLSFASFSSM FHAFLSNNRK
LYKKVVELAQ DKGSYFGSLV QDYKVYSLEM MARQTSSTEM LQEIRTMMTQ LKSYLLQSTE
LKALVDPALH SEEELEAIVE SALYKCVLKP LKEAINSCLH QIHSKDGSLQ QLKENQLVIL
ATTTTDLGVT TSVPEVPMME KILQKFTSMH KAYSPEKKIS ILLKTCKLIY DSMALGNPGK
PYGADDFLPV LMYVLARSNL TEMLLNVEYM MELMDPALQL GEGSYYLTTT YGALEHIKSY
DKITVTRQLS VEVQDSIHRW ERRRTLNKAR ASRSSVQDFI CVSYLEPEQQ ARTLASRADT
QAQALCAQCA EKFAVERPQA HRLFVLVDGR CFQLADDALP HCIKGYLLRS EPKRDFHFVY
RPLDGGGGGG GGSPPCLVVR EPNFL
