ID   PKHM1_MOUSE             Reviewed;        1074 AA.
AC   Q7TSI1; Q3U3L2; Q8CHU5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   22-FEB-2023, entry version 137.
DE   RecName: Full=Pleckstrin homology domain-containing family M member 1 {ECO:0000305};
DE            Short=PH domain-containing family M member 1;
GN   Name=Plekhm1 {ECO:0000312|MGI:MGI:2443207};
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 [LARGE SCALE MRNA].
RC   STRAIN=NOD;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-436 AND SER-491, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Spleen;
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   INTERACTION WITH PAFAH1B1.
RX   PubMed=22073305; DOI=10.1371/journal.pone.0027285;
RA   Ye S., Fowler T.W., Pavlos N.J., Ng P.Y., Liang K., Feng Y., Zheng M.,
RA   Kurten R., Manolagas S.C., Zhao H.;
RT   "LIS1 regulates osteoclast formation and function through its interactions
RT   with dynein/dynactin and Plekhm1.";
RL   PLoS ONE 6:E27285-E27285(2011).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25498145; DOI=10.1016/j.molcel.2014.11.006;
RA   McEwan D.G., Popovic D., Gubas A., Terawaki S., Suzuki H., Stadel D.,
RA   Coxon F.P., Miranda de Stegmann D., Bhogaraju S., Maddi K., Kirchof A.,
RA   Gatti E., Helfrich M.H., Wakatsuki S., Behrends C., Pierre P., Dikic I.;
RT   "PLEKHM1 regulates autophagosome-lysosome fusion through HOPS complex and
RT   LC3/GABARAP proteins.";
RL   Mol. Cell 57:39-54(2015).
RN   [7]
RP   FUNCTION, INTERACTION WITH DEF8; FAM98A; NDEL1 AND RAB7A, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF ARG-714 AND 949-TYR-LEU-950.
RX   PubMed=27777970; DOI=10.1172/jci.insight.86330;
RA   Fujiwara T., Ye S., Castro-Gomes T., Winchell C.G., Andrews N.W.,
RA   Voth D.E., Varughese K.I., Mackintosh S.G., Feng Y., Pavlos N.,
RA   Nakamura T., Manolagas S.C., Zhao H.;
RT   "PLEKHM1/DEF8/RAB7 complex regulates lysosome positioning and bone
RT   homeostasis.";
RL   JCI Insight 1:E86330-E86330(2016).
CC   -!- FUNCTION: Acts as a multivalent adapter protein that regulates Rab7-
CC       dependent and HOPS complex-dependent fusion events in the endolysosomal
CC       system and couples autophagic and the endocytic trafficking pathways.
CC       Acts as a dual effector of RAB7A and ARL8B that simultaneously binds
CC       these GTPases, bringing about clustering and fusion of late endosomes
CC       and lysosomes. Required for late stages of endolysosomal maturation,
CC       facilitating both endocytosis-mediated degradation of growth factor
CC       receptors and autophagosome clearance. Interaction with Arl8b is a
CC       crucial factor in the terminal maturation of autophagosomes and to
CC       mediate autophagosome-lysosome fusion (PubMed:25498145). Positively
CC       regulates lysosome peripheral distribution and ruffled border formation
CC       in osteoclasts (PubMed:27777970). May be involved in negative
CC       regulation of endocytic transport from early endosome to late
CC       endosome/lysosome implicating its association with Rab7. May have a
CC       role in sialyl-lex-mediated transduction of apoptotic signals (By
CC       similarity). Involved in bone resorption (PubMed:27777970).
CC       {ECO:0000250|UniProtKB:Q9Y4G2, ECO:0000269|PubMed:25498145,
CC       ECO:0000269|PubMed:27777970}.
CC   -!- SUBUNIT: Interacts (via N- and C-terminus) with RAB7A (GTP-bound form).
CC       Simultaneously interacts with RAB7A and ARL8B; bringing about
CC       clustering and fusion of late endosomes and lysosomes. Interacts (via
CC       RUN domain) with ARL8B (GTP-bound form); the interaction is required
CC       for PLEKHM1 localization to lysosomes and for ARL8B function in
CC       delivery and degradation of endocytic and autophagic cargo in
CC       lysosomes. PLEKHM1 and PLEKHM2 compete for interaction with ARL8B.
CC       Interacts with ARL8A; the interaction is weaker than with ARL8B.
CC       Interacts with VPS41, VPS11, VPS18, VPS33A and VPS39; indicative for an
CC       association with the HOPS complex; the interactions with, at least,
CC       VPS41, VPS11, VPS18 and VPS33A require ARL8B (By similarity). Interacts
CC       with GABARAP, GABARAPL, GABARAPL2, MAP1LC3A, MAP1LC3B and MAP1LC3C (By
CC       similarity). Interacts with PAFAH1B (PubMed:22073305). Interacts (via
CC       N- and C-terminus) with NDEL1 (PubMed:27777970). Interacts (via C-
CC       terminus) with MAP3K7 (PubMed:27777970). Interacts (via N- and C-
CC       terminus) with FAM98A (PubMed:27777970). Interacts (via C-terminus)
CC       with DEF8; this interaction is weak but increased in a RAB7A-dependent
CC       manner (PubMed:27777970). May interact with sialyl-lex-positive protein
CC       (By similarity). {ECO:0000250|UniProtKB:Q9Y4G2,
CC       ECO:0000269|PubMed:22073305, ECO:0000269|PubMed:27777970}.
CC   -!- SUBCELLULAR LOCATION: Autolysosome membrane
CC       {ECO:0000250|UniProtKB:Q9Y4G2}. Endosome membrane
CC       {ECO:0000250|UniProtKB:Q9Y4G2}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9Y4G2}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q9Y4G2}. Note=In case of infection colocalizes
CC       with Salmonella typhimurium sifA in proximity of Salmonella-containing
CC       vacuole (SCV). {ECO:0000250|UniProtKB:Q9Y4G2}.
CC   -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction
CC       with ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and LC3A/B/C.
CC       {ECO:0000250|UniProtKB:Q9Y4G2}.
CC   -!- DISRUPTION PHENOTYPE: Osteoclast-specific conditional knockout mice
CC       show normal tooth eruption, developed normally and are fertile, but
CC       trabecular bone mass in long bones and vertebrae is increased
CC       (PubMed:27777970). Osteoclast differentiation and number are normal,
CC       but bone resorption is decreased (PubMed:27777970). Show
CC       mislocalization of osteoclast lysosomes at the perinuclear area,
CC       instead at the cell periphery, and decreased ruffled border formation
CC       (PubMed:27777970). {ECO:0000269|PubMed:27777970}.
CC   -!- MISCELLANEOUS: Sialyl-lex is a carcinoma associated antigen.
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DR   EMBL; AK154703; BAE32773.1; -; mRNA.
DR   EMBL; AL772325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038943; AAH38943.1; -; mRNA.
DR   EMBL; BC053079; AAH53079.1; -; mRNA.
DR   CCDS; CCDS25518.1; -.
DR   RefSeq; NP_898855.1; NM_183034.1.
DR   AlphaFoldDB; Q7TSI1; -.
DR   SMR; Q7TSI1; -.
DR   BioGRID; 237251; 1.
DR   IntAct; Q7TSI1; 1.
DR   STRING; 10090.ENSMUSP00000047327; -.
DR   iPTMnet; Q7TSI1; -.
DR   PhosphoSitePlus; Q7TSI1; -.
DR   EPD; Q7TSI1; -.
DR   jPOST; Q7TSI1; -.
DR   MaxQB; Q7TSI1; -.
DR   PaxDb; Q7TSI1; -.
DR   PeptideAtlas; Q7TSI1; -.
DR   ProteomicsDB; 289911; -.
DR   Antibodypedia; 30012; 146 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000041272.10; ENSMUSP00000047327.9; ENSMUSG00000034247.10.
DR   GeneID; 353047; -.
DR   KEGG; mmu:353047; -.
DR   UCSC; uc007lug.1; mouse.
DR   AGR; MGI:2443207; -.
DR   CTD; 9842; -.
DR   MGI; MGI:2443207; Plekhm1.
DR   VEuPathDB; HostDB:ENSMUSG00000034247; -.
DR   eggNOG; KOG1829; Eukaryota.
DR   GeneTree; ENSGT00940000155111; -.
DR   HOGENOM; CLU_011318_0_0_1; -.
DR   InParanoid; Q7TSI1; -.
DR   OMA; HVLNCDL; -.
DR   OrthoDB; 126314at2759; -.
DR   PhylomeDB; Q7TSI1; -.
DR   TreeFam; TF317067; -.
DR   BioGRID-ORCS; 353047; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Plekhm1; mouse.
DR   PRO; PR:Q7TSI1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q7TSI1; protein.
DR   Bgee; ENSMUSG00000034247; Expressed in granulocyte and 189 other tissues.
DR   ExpressionAtlas; Q7TSI1; baseline and differential.
DR   Genevisible; Q7TSI1; MM.
DR   GO; GO:0044754; C:autolysosome; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061909; P:autophagosome-lysosome fusion; ISS:UniProtKB.
DR   GO; GO:1902774; P:late endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IMP:UniProtKB.
DR   GO; GO:1900029; P:positive regulation of ruffle assembly; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd13321; PH_PLEKHM1; 1.
DR   Gene3D; 1.20.58.900; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR042827; PLEKHM1_PH.
DR   InterPro; IPR025258; RH_dom.
DR   InterPro; IPR004012; Run_dom.
DR   InterPro; IPR037213; Run_dom_sf.
DR   PANTHER; PTHR12326; PLECKSTRIN HOMOLOGY DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12326:SF5; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 1; 1.
DR   Pfam; PF02759; RUN; 1.
DR   Pfam; PF13901; zf-RING_9; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM01175; DUF4206; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00593; RUN; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   SUPFAM; SSF140741; RUN domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasmic vesicle; Endosome; Lysosome; Membrane;
KW   Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW   Repeat; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..1074
FT                   /note="Pleckstrin homology domain-containing family M
FT                   member 1"
FT                   /id="PRO_0000309336"
FT   DOMAIN          40..182
FT                   /note="RUN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT   DOMAIN          551..642
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          701..795
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ZN_FING         1004..1058
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          214..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..1074
FT                   /note="Interaction with RAB7A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G2"
FT   MOTIF           649..655
FT                   /note="LIR"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G2"
FT   COMPBIAS        309..336
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..525
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4G2"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         714
FT                   /note="R->C: No change in osteoclast formation and bone
FT                   resorption."
FT                   /evidence="ECO:0000269|PubMed:27777970"
FT   MUTAGEN         949..950
FT                   /note="YL->AA: Decreases interaction with RAB7A."
FT                   /evidence="ECO:0000269|PubMed:27777970"
FT   CONFLICT        742..744
FT                   /note="DSH -> TRP (in Ref. 3; AAH38943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        768
FT                   /note="T -> S (in Ref. 1; BAE32773)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1074 AA;  118535 MW;  56EDA05514E4B9F9 CRC64;
     MLSVENGLDP RAAIQVIKKK LVGSVKALQK QHVSLDTVVT SEDGDANTMC SALEAVFIHG
     LHAKHIRAEA GGKRKKHTHQ KALPQPVFWP LLKAITHRHI VSDLEHLVFI NTDVGRCRAW
     LRLALNDGLM ECYLKLLLQE PARLCEYYQP TALLRDAEEA EFLLSFLQGL TSLSFELSYK
     SAILNEWTLT PLSLSGLCPL SELDPLTTSG AELQRKESLD SISHSSGSED IEVQHSGHKI
     RRNRKLTASS LSLDTASSSQ LSCSLNSDSC LLQENGPKSP DHSEEPMSYD SDLGMANTDD
     PDRSLQEVLS EFSKAQVNSA PSSGPNQEPD TPMFQTPLSL HSLATSTHLH FEGSEELFPA
     HKSSGTSSGG HKHQLLPQET PDEKQLGTAQ AGPAQSTSDQ QPSSPVGGAA GQGSGPWKAL
     EYGRVGPKLV VSSPTSPKGK SWISEDDFCR PPQEPALKSA AGLCTSPVQD TPESRAALHG
     PFSQGPRKSC SLGALDKACV PSQACGNAQP APAPAPAPAP APAPAPGVTQ DHKNFCVVHR
     RQMGLSNPFR GLMKLGTVAR RGAMGIWKEF FCELSPLEFR LYLSDEERTC VESCSLLRCE
     AVGPAHSDGR FELVFSGKKL ALRASSQDEA EDWLDRVREA LQKVRPQQED EWVNIQYPDQ
     AEDAPEAPPD SLPPYSTLLP EPAGAQGMQL DWTSAQVPEP DAIKESLLYL YADRTWVPYI
     FSLSLESLKC FRVRNNEKML SDSHGVETIR DILPDTSLGG PAFFKIITAK AVLKLQAKNT
     EEATHWRDLV RKVLASYLES AEEAVTLGGS LDEKCQEVLK FATRENGFLL QYLVAIPTEK
     GLDSQGCFCA GCSRQIGFSF VRPKLCAFSG LYYCDFCHQD DASVIPARII HNWDLTKRPV
     CRQALKFLAQ IRAQPLINLQ LVNASLYEHV ERMHLIGRSR EQLKLLGDYL GLCRSGALKE
     LCKRLSHRNY LLESPHRFSV ADLQQIAEGV YEGFLKALIE FASQHVYHCD LCTQRGFICQ
     ICHHQDIIFP FEFDTTVRCA ECRTVFHQSC QAVVRKGCPR CARRRKYQEQ NVVS
//