CEP19_HUMAN
ID CEP19_HUMAN Reviewed; 163 AA.
AC Q96LK0; B2RA74; Q96I48;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Centrosomal protein of 19 kDa;
DE Short=Cep19;
GN Name=CEP19; Synonyms=C3orf34; ORFNames=HSD5;
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].
RC TISSUE=Testis;
RA Wang L.F., Zhang X.D., Miao S.Y., Gou D., Wang Y.;
RT "A new spermatogenesis-related gene.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21399614; DOI=10.1038/emboj.2011.63;
RA Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
RA Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
RA Hyman A.A., Andersen J.S.;
RT "Novel asymmetrically localizing components of human centrosomes identified
RT by complementary proteomics methods.";
RL EMBO J. 30:1520-1535(2011).
RN [6]
RP INVOLVEMENT IN MOSPGF, AND SUBCELLULAR LOCATION.
RX PubMed=24268657; DOI=10.1016/j.ajhg.2013.10.025;
RA Shalata A., Ramirez M.C., Desnick R.J., Priedigkeit N., Buettner C.,
RA Lindtner C., Mahroum M., Abdul-Ghani M., Dong F., Arar N.,
RA Camacho-Vanegas O., Zhang R., Camacho S.C., Chen Y., Ibdah M., DeFronzo R.,
RA Gillespie V., Kelley K., Dynlacht B.D., Kim S., Glucksman M.J.,
RA Borochowitz Z.U., Martignetti J.A.;
RT "Morbid obesity resulting from inactivation of the ciliary protein CEP19 in
RT humans and mice.";
RL Am. J. Hum. Genet. 93:1061-1071(2013).
RN [7]
RP FUNCTION, INTERACTION WITH CEP43 AND RABL2B, SUBCELLULAR LOCATION, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016;
RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.;
RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar
RT transport at the ciliary base.";
RL Dev. Cell 42:1-15(2017).
RN [8]
RP FUNCTION, INTERACTION WITH CEP43 AND RABL2B, AND SUBCELLULAR LOCATION.
RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017;
RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.;
RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and
RT participates in ciliary assembly.";
RL Mol. Biol. Cell 28:1652-1666(2017).
RN [9]
RP FUNCTION, INTERACTION WITH CEP43 AND CEP350, AND SUBCELLULAR LOCATION.
RX PubMed=28659385; DOI=10.1098/rsob.170114;
RA Mojarad B.A., Gupta G.D., Hasegan M., Goudiam O., Basto R., Gingras A.C.,
RA Pelletier L.;
RT "CEP19 cooperates with FOP and CEP350 to drive early steps in the
RT ciliogenesis programme.";
RL Open Biol. 7:0-0(2017).
CC -!- FUNCTION: Required for ciliation (PubMed:28625565, PubMed:28428259,
CC PubMed:28659385). Recruits the RABL2B GTPase to the ciliary base to
CC initiate ciliation. After specifically capturing the activated GTP-
CC bound RABL2B, the CEP19-RABL2B complex binds intraflagellar transport
CC (IFT) complex B from the large pool pre-docked at the base of the
CC cilium and thus triggers its entry into the cilia (PubMed:28625565,
CC PubMed:28428259). Involved in the early steps in cilia formation by
CC recruiting the ciliary vesicles (CVs) to the distal end of the mother
CC centriole where they fuse to initiate cilium assembly. Involved in
CC microtubule (MT) anchoring to the centrosomes (PubMed:28659385).
CC {ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565,
CC ECO:0000269|PubMed:28659385}.
CC -!- SUBUNIT: Interacts with CEP43; this interaction is required for its
CC localization to the mother centriole (PubMed:28625565, PubMed:28428259,
CC PubMed:28659385). Interacts (via residues 121-150) with RABL2B
CC (PubMed:28625565, PubMed:28428259). Interacts (via C-terminus) with
CC CEP350; this interaction is required for its localization to the mother
CC centriole (PubMed:28659385). {ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
CC -!- INTERACTION:
CC Q96LK0; P60006: ANAPC15; NbExp=3; IntAct=EBI-741885, EBI-8787535;
CC Q96LK0; Q8IY42: C4orf19; NbExp=3; IntAct=EBI-741885, EBI-10216552;
CC Q96LK0; Q9P1Z2: CALCOCO1; NbExp=6; IntAct=EBI-741885, EBI-749920;
CC Q96LK0; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-741885, EBI-10171570;
CC Q96LK0; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-741885, EBI-711501;
CC Q96LK0; Q96AQ1: CCDC74A; NbExp=3; IntAct=EBI-741885, EBI-8466689;
CC Q96LK0; P51861: CDR1; NbExp=3; IntAct=EBI-741885, EBI-2836538;
CC Q96LK0; O95684: CEP43; NbExp=6; IntAct=EBI-741885, EBI-1266334;
CC Q96LK0; O95684-2: CEP43; NbExp=7; IntAct=EBI-741885, EBI-1266347;
CC Q96LK0; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-741885, EBI-852194;
CC Q96LK0; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-741885, EBI-742054;
CC Q96LK0; O60447: EVI5; NbExp=3; IntAct=EBI-741885, EBI-852291;
CC Q96LK0; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-741885, EBI-10253815;
CC Q96LK0; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-741885, EBI-948296;
CC Q96LK0; Q9BVP2: GNL3; NbExp=4; IntAct=EBI-741885, EBI-641642;
CC Q96LK0; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-741885, EBI-10175326;
CC Q96LK0; Q16082: HSPB2; NbExp=6; IntAct=EBI-741885, EBI-739395;
CC Q96LK0; Q8N8K9: KIAA1958; NbExp=3; IntAct=EBI-741885, EBI-10181113;
CC Q96LK0; Q9BQD3: KXD1; NbExp=7; IntAct=EBI-741885, EBI-739657;
CC Q96LK0; Q8IV50-2: LYSMD2; NbExp=3; IntAct=EBI-741885, EBI-19761491;
CC Q96LK0; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-741885, EBI-17490746;
CC Q96LK0; O95340: PAPSS2; NbExp=6; IntAct=EBI-741885, EBI-1053912;
CC Q96LK0; Q92968: PEX13; NbExp=3; IntAct=EBI-741885, EBI-594849;
CC Q96LK0; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-741885, EBI-14066006;
CC Q96LK0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-741885, EBI-79165;
CC Q96LK0; Q92569: PIK3R3; NbExp=4; IntAct=EBI-741885, EBI-79893;
CC Q96LK0; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-741885, EBI-949945;
CC Q96LK0; Q96NZ9: PRAP1; NbExp=3; IntAct=EBI-741885, EBI-2116102;
CC Q96LK0; P31321: PRKAR1B; NbExp=5; IntAct=EBI-741885, EBI-2805516;
CC Q96LK0; Q9H3S7: PTPN23; NbExp=3; IntAct=EBI-741885, EBI-724478;
CC Q96LK0; Q9UBK7-2: RABL2A; NbExp=6; IntAct=EBI-741885, EBI-4402837;
CC Q96LK0; Q9UNT1-2: RABL2B; NbExp=3; IntAct=EBI-741885, EBI-12256104;
CC Q96LK0; Q04864: REL; NbExp=3; IntAct=EBI-741885, EBI-307352;
CC Q96LK0; Q04864-2: REL; NbExp=3; IntAct=EBI-741885, EBI-10829018;
CC Q96LK0; Q8WZ75: ROBO4; NbExp=3; IntAct=EBI-741885, EBI-6508018;
CC Q96LK0; Q9H4L4: SENP3; NbExp=3; IntAct=EBI-741885, EBI-2880236;
CC Q96LK0; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-741885, EBI-748621;
CC Q96LK0; Q8N205: SYNE4; NbExp=3; IntAct=EBI-741885, EBI-7131783;
CC Q96LK0; Q8N205-2: SYNE4; NbExp=3; IntAct=EBI-741885, EBI-12099160;
CC Q96LK0; P19237: TNNI1; NbExp=3; IntAct=EBI-741885, EBI-746692;
CC Q96LK0; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-741885, EBI-1756205;
CC Q96LK0; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-741885, EBI-947459;
CC Q96LK0; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-741885, EBI-11343401;
CC Q96LK0; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-741885, EBI-6116822;
CC Q96LK0; P55072: VCP; NbExp=3; IntAct=EBI-741885, EBI-355164;
CC Q96LK0; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-741885, EBI-2799833;
CC Q96LK0; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-741885, EBI-12017160;
CC Q96LK0; O43829: ZBTB14; NbExp=6; IntAct=EBI-741885, EBI-10176632;
CC Q96LK0; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-741885, EBI-2555749;
CC Q96LK0; Q8TAQ5: ZNF420; NbExp=3; IntAct=EBI-741885, EBI-3923307;
CC Q96LK0; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-741885, EBI-11962468;
CC Q96LK0; Q6ZT36; NbExp=5; IntAct=EBI-741885, EBI-13335465;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565,
CC ECO:0000269|PubMed:28659385}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:21399614}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:24268657, ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
CC Note=Associates with the mother centriole in early interphase.
CC Localizes to spindle poles during mitosis, and to distinct foci
CC oriented towards the midbody at telophase (PubMed:21399614). Localizes
CC slightly apical to the subdistal appendage on the mother centriole, but
CC below the distal appendage (PubMed:28625565, PubMed:28659385).
CC {ECO:0000269|PubMed:21399614, ECO:0000269|PubMed:28625565}.
CC -!- DISEASE: Morbid obesity and spermatogenic failure (MOSPGF)
CC [MIM:615703]: An autosomal recessive morbid obesity syndrome
CC characterized by hypertension, fatty liver disease, insulin resistance,
CC and decreased sperm counts. Variable clinical manifestations are early
CC coronary artery disease with myocardial infarction before 45 years of
CC age, type II diabetes mellitus, and intellectual disability. Morbid
CC obese individuals are defined as having a BMI greater than 40.
CC {ECO:0000269|PubMed:24268657}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CEP19 family. {ECO:0000305}.
CC -!- CAUTION: The region that interacts with CEP43 is conflicting: According
CC to a report, interacts via N-terminus (PubMed:28428259). According to
CC another report, interacts via C-terminus (PubMed:28659385).
CC {ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28659385}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM47487.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71691.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY099509; AAM47487.1; ALT_INIT; mRNA.
DR EMBL; AK058155; BAB71691.1; ALT_INIT; mRNA.
DR EMBL; AK314070; BAG36771.1; -; mRNA.
DR EMBL; AC055725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007827; AAH07827.1; -; mRNA.
DR CCDS; CCDS43193.2; -.
DR RefSeq; NP_116287.2; NM_032898.4.
DR RefSeq; XP_005269427.1; XM_005269370.4.
DR RefSeq; XP_011511548.1; XM_011513246.2.
DR AlphaFoldDB; Q96LK0; -.
DR BioGRID; 124410; 158.
DR IntAct; Q96LK0; 141.
DR STRING; 9606.ENSP00000387209; -.
DR MoonDB; Q96LK0; Predicted.
DR PhosphoSitePlus; Q96LK0; -.
DR BioMuta; CEP19; -.
DR DMDM; 115503728; -.
DR MassIVE; Q96LK0; -.
DR PaxDb; Q96LK0; -.
DR PeptideAtlas; Q96LK0; -.
DR PRIDE; Q96LK0; -.
DR ProteomicsDB; 77216; -.
DR Antibodypedia; 33949; 69 antibodies from 18 providers.
DR DNASU; 84984; -.
DR Ensembl; ENST00000409690.5; ENSP00000387209.4; ENSG00000174007.9.
DR GeneID; 84984; -.
DR KEGG; hsa:84984; -.
DR MANE-Select; ENST00000409690.5; ENSP00000387209.4; NM_032898.5; NP_116287.3.
DR UCSC; uc011btw.3; human.
DR CTD; 84984; -.
DR DisGeNET; 84984; -.
DR GeneCards; CEP19; -.
DR HGNC; HGNC:28209; CEP19.
DR HPA; ENSG00000174007; Low tissue specificity.
DR MalaCards; CEP19; -.
DR MIM; 615586; gene.
DR MIM; 615703; phenotype.
DR neXtProt; NX_Q96LK0; -.
DR OpenTargets; ENSG00000174007; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR Orphanet; 397615; Obesity due to CEP19 deficiency.
DR PharmGKB; PA142672395; -.
DR VEuPathDB; HostDB:ENSG00000174007; -.
DR eggNOG; ENOG502RZP1; Eukaryota.
DR GeneTree; ENSGT00390000016356; -.
DR HOGENOM; CLU_113348_0_0_1; -.
DR InParanoid; Q96LK0; -.
DR OMA; QEKCSWD; -.
DR OrthoDB; 1594443at2759; -.
DR PhylomeDB; Q96LK0; -.
DR TreeFam; TF328425; -.
DR PathwayCommons; Q96LK0; -.
DR SignaLink; Q96LK0; -.
DR BioGRID-ORCS; 84984; 11 hits in 1076 CRISPR screens.
DR GenomeRNAi; 84984; -.
DR Pharos; Q96LK0; Tbio.
DR PRO; PR:Q96LK0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96LK0; protein.
DR Bgee; ENSG00000174007; Expressed in blood and 151 other tissues.
DR ExpressionAtlas; Q96LK0; baseline and differential.
DR Genevisible; Q96LK0; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:UniProtKB.
DR GO; GO:0097712; P:vesicle targeting, trans-Golgi to periciliary membrane compartment; IMP:UniProtKB.
DR InterPro; IPR029412; CEP19.
DR PANTHER; PTHR31539; PTHR31539; 2.
DR Pfam; PF14933; CEP19; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Obesity; Reference proteome.
FT CHAIN 1..163
FT /note="Centrosomal protein of 19 kDa"
FT /id="PRO_0000251960"
SQ SEQUENCE 163 AA; 19166 MW; D5F65C3C0A1B1AD7 CRC64;
MMCTAKKCGI RFQPPAIILI YESEIKGKIR QRIMPVRNFS KFSDCTRAAE QLKNNPRHKS
YLEQVSLRQL EKLFSFLRGY LSGQSLAETM EQIQRETTID PEEDLNKLDD KELAKRKSIM
DELFEKNQKK KDDPNFVYDI EVEFPQDDQL QSCGWDTESA DEF
