RAB34_HUMAN
ID RAB34_HUMAN Reviewed; 259 AA.
AC Q9BZG1; B4E3A0; E9PEJ9; Q5BJE6; Q8NCJ8; Q96AR4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Ras-related protein Rab-34;
DE AltName: Full=Ras-related protein Rab-39;
DE AltName: Full=Ras-related protein Rah;
GN Name=RAB34; Synonyms=RAB39, RAH;
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).
RA Hong W.;
RT "Human Rab39 coding region (cDNA).";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Stanchi F., Lanfranchi G.;
RT "Full-length sequencing of 100 cDNA clones from human adult skeletal
RT muscle.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Embryo, Mammary gland, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas;
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 [7]
RP INTERACTION WITH RILP.
RX PubMed=14668488; DOI=10.1091/mbc.e03-06-0413;
RA Wang T., Wong K.K., Hong W.;
RT "A unique region of RILP distinguishes it from its related proteins in its
RT regulation of lysosomal morphology and interaction with Rab7 and Rab34.";
RL Mol. Biol. Cell 15:815-826(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21255211; DOI=10.1111/j.1600-0854.2011.01165.x;
RA Seto S., Tsujimura K., Koide Y.;
RT "Rab GTPases regulating phagosome maturation are differentially recruited
RT to mycobacterial phagosomes.";
RL Traffic 12:407-420(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, AND INTERACTION WITH RILP.
RX PubMed=27113757; DOI=10.15252/embr.201541382;
RA Starling G.P., Yip Y.Y., Sanger A., Morton P.E., Eden E.R., Dodding M.P.;
RT "Folliculin directs the formation of a Rab34-RILP complex to control the
RT nutrient-dependent dynamic distribution of lysosomes.";
RL EMBO Rep. 17:823-841(2016).
CC -!- FUNCTION: Transport protein involved in the redistribution of lysosomes
CC to the peri-Golgi region (PubMed:27113757). Plays a role in the
CC maturation of phagosomes that engulf pathogens, such as S.aureus and
CC M.tuberculosis (PubMed:21255211). Plays a role in the fusion of
CC phagosomes with lysosomes (PubMed:21255211). Acts also as a positive
CC regulator of hedgehog signaling and regulates ciliary function (By
CC similarity). {ECO:0000250|UniProtKB:Q64008,
CC ECO:0000269|PubMed:21255211, ECO:0000269|PubMed:27113757}.
CC -!- SUBUNIT: Interacts with RILP. {ECO:0000269|PubMed:14668488,
CC ECO:0000269|PubMed:27113757}.
CC -!- INTERACTION:
CC Q9BZG1; P35219: CA8; NbExp=3; IntAct=EBI-2856739, EBI-718700;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64008}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q64008}. Cytoplasmic vesicle,
CC phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000269|PubMed:21255211}; Lipid-anchor
CC {ECO:0000269|PubMed:21255211}; Cytoplasmic side
CC {ECO:0000269|PubMed:21255211}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q64008}. Note=Recruited to phagosomes containing
CC S.aureus or M.tuberculosis (PubMed:21255211).
CC {ECO:0000269|PubMed:21255211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BZG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZG1-2; Sequence=VSP_010142;
CC Name=NARR;
CC IsoId=P0DI83-1; Sequence=External;
CC Name=4;
CC IsoId=Q9BZG1-4; Sequence=VSP_044734;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF322067; AAK09397.1; -; mRNA.
DR EMBL; AJ277106; CAC81760.1; -; mRNA.
DR EMBL; BT006702; AAP35348.1; -; mRNA.
DR EMBL; AK027312; BAB55034.1; -; mRNA.
DR EMBL; AK074689; BAC11141.1; -; mRNA.
DR EMBL; AK304633; BAG65412.1; -; mRNA.
DR EMBL; AC010761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016841; AAH16841.1; -; mRNA.
DR EMBL; BC091510; AAH91510.1; -; mRNA.
DR CCDS; CCDS11240.1; -. [Q9BZG1-1]
DR CCDS; CCDS45636.1; -. [Q9BZG1-2]
DR CCDS; CCDS58536.1; -. [Q9BZG1-4]
DR RefSeq; NP_001138414.1; NM_001144942.1. [Q9BZG1-2]
DR RefSeq; NP_001243205.1; NM_001256276.1. [Q9BZG1-4]
DR RefSeq; NP_001243206.1; NM_001256277.1. [Q9BZG1-1]
DR RefSeq; NP_001243207.1; NM_001256278.1.
DR RefSeq; NP_114140.4; NM_031934.5. [Q9BZG1-1]
DR AlphaFoldDB; Q9BZG1; -.
DR SMR; Q9BZG1; -.
DR BioGRID; 123784; 57.
DR IntAct; Q9BZG1; 29.
DR MINT; Q9BZG1; -.
DR STRING; 9606.ENSP00000413156; -.
DR iPTMnet; Q9BZG1; -.
DR PhosphoSitePlus; Q9BZG1; -.
DR BioMuta; RAB34; -.
DR DMDM; 20139693; -.
DR EPD; Q9BZG1; -.
DR jPOST; Q9BZG1; -.
DR MassIVE; Q9BZG1; -.
DR MaxQB; Q9BZG1; -.
DR PaxDb; Q9BZG1; -.
DR PeptideAtlas; Q9BZG1; -.
DR PRIDE; Q9BZG1; -.
DR ProteomicsDB; 19907; -.
DR ProteomicsDB; 79837; -. [Q9BZG1-1]
DR ProteomicsDB; 79838; -. [Q9BZG1-2]
DR Antibodypedia; 14281; 127 antibodies from 26 providers.
DR DNASU; 83871; -.
DR Ensembl; ENST00000301043.10; ENSP00000301043.6; ENSG00000109113.20. [Q9BZG1-1]
DR Ensembl; ENST00000395245.9; ENSP00000378666.3; ENSG00000109113.20. [Q9BZG1-1]
DR Ensembl; ENST00000415040.6; ENSP00000410279.2; ENSG00000109113.20. [Q9BZG1-4]
DR Ensembl; ENST00000436730.7; ENSP00000404180.3; ENSG00000109113.20. [Q9BZG1-1]
DR Ensembl; ENST00000450529.5; ENSP00000391048.1; ENSG00000109113.20. [Q9BZG1-2]
DR GeneID; 83871; -.
DR KEGG; hsa:83871; -.
DR MANE-Select; ENST00000395245.9; ENSP00000378666.3; NM_031934.6; NP_114140.4.
DR UCSC; uc002hce.3; human. [Q9BZG1-1]
DR CTD; 83871; -.
DR DisGeNET; 83871; -.
DR GeneCards; RAB34; -.
DR HGNC; HGNC:16519; RAB34.
DR HPA; ENSG00000109113; Low tissue specificity.
DR MIM; 610917; gene.
DR neXtProt; NX_Q9BZG1; -.
DR OpenTargets; ENSG00000109113; -.
DR PharmGKB; PA34126; -.
DR VEuPathDB; HostDB:ENSG00000109113; -.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000159645; -.
DR InParanoid; Q9BZG1; -.
DR OMA; KKKQANC; -.
DR OrthoDB; 1048146at2759; -.
DR PhylomeDB; Q9BZG1; -.
DR PathwayCommons; Q9BZG1; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q9BZG1; -.
DR BioGRID-ORCS; 83871; 25 hits in 1081 CRISPR screens.
DR ChiTaRS; RAB34; human.
DR GeneWiki; RAB34; -.
DR GenomeRNAi; 83871; -.
DR Pharos; Q9BZG1; Tbio.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BZG1; protein.
DR Bgee; ENSG00000109113; Expressed in descending thoracic aorta and 174 other tissues.
DR ExpressionAtlas; Q9BZG1; baseline and differential.
DR Genevisible; Q9BZG1; HS.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; IDA:UniProtKB.
DR GO; GO:0090382; P:phagosome maturation; IMP:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..259
FT /note="Ras-related protein Rab-34"
FT /id="PRO_0000121243"
FT MOTIF 81..89
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 107..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 166..169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT LIPID 257
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 258
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 51..72
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044734"
FT VAR_SEQ 164..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_010142"
FT VARIANT 197
FT /note="V -> L (in dbSNP:rs12125)"
FT /id="VAR_015097"
FT CONFLICT 10
FT /note="D -> Y (in Ref. 4; BAG65412)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> I (in Ref. 4; BAC11141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29044 MW; 6D38A6F090F9802D CRC64;
MNILAPVRRD RVLAELPQCL RKEAALHGHK DFHPRVTCAC QEHRTGTVGF KISKVIVVGD
LSVGKTCLIN RFCKDTFDKN YKATIGVDFE MERFEVLGIP FSLQLWDTAG QERFKCIAST
YYRGAQAIII VFNLNDVASL EHTKQWLADA LKENDPSSVL LFLVGSKKDL STPAQYALME
KDALQVAQEM KAEYWAVSSL TGENVREFFF RVAALTFEAN VLAELEKSGA RRIGDVVRIN
SDDSNLYLTA SKKKPTCCP
