GCNA_HUMAN
ID GCNA_HUMAN Reviewed; 691 AA.
AC Q96QF7; B9EG62;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Germ cell nuclear acidic protein {ECO:0000305};
DE AltName: Full=Acidic repeat-containing protein {ECO:0000303|PubMed:11714101};
DE AltName: Full=Germ cell nuclear acidic peptidase {ECO:0000303|PubMed:34413498};
DE AltName: Full=Germ cell nuclear antigen {ECO:0000303|PubMed:27718356};
GN Name=GCNA {ECO:0000312|HGNC:HGNC:15805};
GN Synonyms=ACRC {ECO:0000303|PubMed:11714101};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11714101; DOI=10.1007/s100480100120;
RA Nolte D., Ramser J., Niemann S., Lehrach H., Sudbrak R., Mueller U.;
RT "ACRC codes for a novel nuclear protein with unusual acidic repeat tract
RT and maps to DYT3 (dystonia parkinsonism) critical interval in xq13.1.";
RL Neurogenetics 3:207-213(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Heart, and 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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27718356; DOI=10.7554/elife.19993;
RA Carmell M.A., Dokshin G.A., Skaletsky H., Hu Y.C., van Wolfswinkel J.C.,
RA Igarashi K.J., Bellott D.W., Nefedov M., Reddien P.W., Enders G.C.,
RA Uversky V.N., Mello C.C., Page D.C.;
RT "A widely employed germ cell marker is an ancient disordered protein with
RT reproductive functions in diverse eukaryotes.";
RL Elife 5:0-0(2016).
RN [5]
RP INTERACTION WITH SUMO2, MUTAGENESIS OF 22-ILE--VAL-25; 76-VAL--ILE-79;
RP 97-LEU--ILE-100 AND 121-ILE--SER-124, IDENTIFICATION OF REPEAT
RP SUMO-INTERACTING MOTIF, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=30914427; DOI=10.15252/embj.2019101496;
RA Borgermann N., Ackermann L., Schwertman P., Hendriks I.A., Thijssen K.,
RA Liu J.C., Lans H., Nielsen M.L., Mailand N.;
RT "SUMOylation promotes protective responses to DNA-protein cross-links.";
RL EMBO J. 38:0-0(2019).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS ASN-17; MET-76;
RP ARG-102; LYS-182; SER-189; ASN-218; PRO-285; PRO-295; SER-441; ILE-465;
RP SER-545; TRP-659; CYS-664 AND CYS-686.
RX PubMed=33963445; DOI=10.1007/s00439-021-02287-y;
RG GEMINI Consortium;
RA Hardy J.J., Wyrwoll M.J., Mcfadden W., Malcher A., Rotte N., Pollock N.C.,
RA Munyoki S., Veroli M.V., Houston B.J., Xavier M.J., Kasak L., Punab M.,
RA Laan M., Kliesch S., Schlegel P., Jaffe T., Hwang K., Vukina J.,
RA Brieno-Enriquez M.A., Orwig K., Yanowitz J., Buszczak M., Veltman J.A.,
RA Oud M., Nagirnaja L., Olszewska M., O'Bryan M.K., Conrad D.F., Kurpisz M.,
RA Tuettelmann F., Yatsenko A.N.;
RT "Variants in GCNA, X-linked germ-cell genome integrity gene, identified in
RT men with primary spermatogenic failure.";
RL Hum. Genet. 140:1169-1182(2021).
RN [7]
RP VARIANTS SER-218 AND GLU-394 DEL.
RX PubMed=34413498; DOI=10.1038/s41431-021-00946-2;
RA Arafat M., Kleiman S.E., AbuMadighem A., Zeadna A., Levitas E., Vardi I.H.,
RA Barda S., Lehavi O., Hauser R., Lunenfeld E., Huleihel M., Gershoni M.,
RA Parvari R.;
RT "Pathogenic variations in Germ Cell Nuclear Acidic Peptidase (GCNA) are
RT associated with human male infertility.";
RL Eur. J. Hum. Genet. 29:1781-1788(2021).
CC -!- FUNCTION: May play a role in DNA-protein cross-links (DPCs) clearance
CC through a SUMO-dependent recruitment to sites of DPCs, ensuring the
CC genomic stability by protecting germ cells and early embryos from
CC various sources of damage (PubMed:30914427). Can resolve the
CC topoisomerase II (TOP2A) DPCs (By similarity).
CC {ECO:0000250|UniProtKB:A0A1D9BZF0, ECO:0000269|PubMed:30914427}.
CC -!- SUBUNIT: Interacts (via SIM domains) with SUMO2; this interaction
CC allows the GCNA recruitment to DPCs sites (PubMed:30914427). Interacts
CC with TOP2A; this interaction allows the resolution of topoisomerase II
CC (TOP2A) DNA-protein cross-links (By similarity).
CC {ECO:0000250|UniProtKB:A0A1D9BZF0, ECO:0000269|PubMed:30914427}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27718356,
CC ECO:0000305|PubMed:11714101}. Nucleus, PML body
CC {ECO:0000269|PubMed:30914427}. Chromosome
CC {ECO:0000250|UniProtKB:A0A1D9BZF0}. Note=Co-localizes with SUMO2 at PML
CC bodies in all interphase cells (PubMed:30914427). Localizes on
CC condensed chromosomes in spermatocytes in G2 and M during meiotic
CC prophase (By similarity). {ECO:0000250|UniProtKB:A0A1D9BZF0,
CC ECO:0000269|PubMed:30914427}.
CC -!- TISSUE SPECIFICITY: Expressed in germ cells of the testis (at protein
CC level) (PubMed:27718356). Detected in skeletal muscle, liver, kidney,
CC pancreas, heart, lung and brain (PubMed:11714101). Expressed throughout
CC spermatogenesis, from spermatogonia to elongated spermatids, in normal
CC adult testis (at protein level) (PubMed:33963445).
CC {ECO:0000269|PubMed:11714101, ECO:0000269|PubMed:27718356,
CC ECO:0000269|PubMed:33963445}.
CC -!- DOMAIN: SUMO interaction motif 1 (SIM) mediates the binding to
CC polysumoylated substrates. {ECO:0000269|PubMed:30914427}.
CC -!- DISEASE: Note=Defects in GCNA are associated with spermatogenic failure
CC (SPGF) such as non-obstructive azoospermia (NOA) and cryptozoospermia.
CC NOA is characterized by no sperm in the ejaculate due to impaired sperm
CC production. Cryptozoospermia is characterized by no sperm in fresh
CC ejaculate without evidence of partial reproductive tract obstruction,
CC but with rare sperm seen in centrifuged pellet.
CC {ECO:0000269|PubMed:33963445}.
CC -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC (SDr) family. {ECO:0000305}.
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DR EMBL; AJ311392; CAC60255.1; -; mRNA.
DR EMBL; AK097433; BAC05051.1; -; mRNA.
DR EMBL; BC136259; AAI36260.1; -; mRNA.
DR CCDS; CCDS35326.1; -.
DR RefSeq; NP_443189.1; NM_052957.4.
DR RefSeq; XP_006724779.1; XM_006724716.3.
DR RefSeq; XP_011529366.1; XM_011531064.1.
DR RefSeq; XP_016885454.1; XM_017029965.1.
DR AlphaFoldDB; Q96QF7; -.
DR BioGRID; 125058; 1.
DR IntAct; Q96QF7; 1.
DR STRING; 9606.ENSP00000362799; -.
DR iPTMnet; Q96QF7; -.
DR PhosphoSitePlus; Q96QF7; -.
DR BioMuta; GCNA; -.
DR DMDM; 74732669; -.
DR MassIVE; Q96QF7; -.
DR PaxDb; Q96QF7; -.
DR PeptideAtlas; Q96QF7; -.
DR PRIDE; Q96QF7; -.
DR ProteomicsDB; 77875; -.
DR Antibodypedia; 13638; 95 antibodies from 18 providers.
DR Ensembl; ENST00000373695.1; ENSP00000362799.1; ENSG00000147174.12.
DR Ensembl; ENST00000373696.8; ENSP00000362800.3; ENSG00000147174.12.
DR GeneID; 93953; -.
DR KEGG; hsa:93953; -.
DR MANE-Select; ENST00000373696.8; ENSP00000362800.3; NM_052957.5; NP_443189.1.
DR UCSC; uc004eae.3; human.
DR CTD; 93953; -.
DR DisGeNET; 93953; -.
DR GeneCards; GCNA; -.
DR HGNC; HGNC:15805; GCNA.
DR HPA; ENSG00000147174; Tissue enhanced (testis).
DR MIM; 300369; gene.
DR neXtProt; NX_Q96QF7; -.
DR OpenTargets; ENSG00000147174; -.
DR PharmGKB; PA24453; -.
DR VEuPathDB; HostDB:ENSG00000147174; -.
DR eggNOG; KOG3854; Eukaryota.
DR GeneTree; ENSGT00440000040163; -.
DR HOGENOM; CLU_026277_0_0_1; -.
DR InParanoid; Q96QF7; -.
DR OMA; SEAPDNN; -.
DR OrthoDB; 1063317at2759; -.
DR PhylomeDB; Q96QF7; -.
DR TreeFam; TF316140; -.
DR PathwayCommons; Q96QF7; -.
DR SignaLink; Q96QF7; -.
DR BioGRID-ORCS; 93953; 7 hits in 698 CRISPR screens.
DR ChiTaRS; ACRC; human.
DR GeneWiki; Acidic_repeat-containing_protein; -.
DR GenomeRNAi; 93953; -.
DR Pharos; Q96QF7; Tbio.
DR PRO; PR:Q96QF7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q96QF7; protein.
DR Bgee; ENSG00000147174; Expressed in ileal mucosa and 117 other tissues.
DR Genevisible; Q96QF7; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0032184; F:SUMO polymer binding; IDA:UniProtKB.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IMP:UniProtKB.
DR InterPro; IPR006640; SprT-like_domain.
DR Pfam; PF10263; SprT-like; 1.
DR SMART; SM00731; SprT; 1.
PE 1: Evidence at protein level;
KW Chromosome; Disease variant; Nucleus; Reference proteome.
FT CHAIN 1..691
FT /note="Germ cell nuclear acidic protein"
FT /id="PRO_0000317387"
FT DOMAIN 522..677
FT /note="SprT-like"
FT REGION 25..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..25
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000269|PubMed:30914427"
FT MOTIF 76..79
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000269|PubMed:30914427"
FT MOTIF 97..100
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000269|PubMed:30914427"
FT MOTIF 121..124
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000269|PubMed:30914427"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..488
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 17
FT /note="D -> N (found in a patient with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs746349614)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085476"
FT VARIANT 76
FT /note="V -> M (found in a patient with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs200457016)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085477"
FT VARIANT 102
FT /note="S -> R (found in a patient with spermatogenic
FT failure; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085478"
FT VARIANT 182
FT /note="N -> K (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs766534592)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085479"
FT VARIANT 189
FT /note="P -> S (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs143368028)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085480"
FT VARIANT 218
FT /note="K -> N (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs141229655)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085481"
FT VARIANT 218
FT /note="K -> S (found in a patient with a severe
FT oligo- astheno-terato-zoospermia; requires 2 nucleotide
FT substitutions; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:34413498"
FT /id="VAR_085482"
FT VARIANT 285
FT /note="S -> P (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs199853865)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085483"
FT VARIANT 295
FT /note="S -> P (found in a patient with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs761086272)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085484"
FT VARIANT 394
FT /note="Missing (found in a patient with azoospermia;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:34413498"
FT /id="VAR_085485"
FT VARIANT 441
FT /note="R -> S (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs144602884)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085486"
FT VARIANT 465
FT /note="T -> I (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs776093985)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085487"
FT VARIANT 471
FT /note="R -> H (in dbSNP:rs10217999)"
FT /id="VAR_050634"
FT VARIANT 545
FT /note="G -> S (found in patients with spermatogenic
FT failure; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085488"
FT VARIANT 659
FT /note="S -> W (found in a patient with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs756204489)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085489"
FT VARIANT 662
FT /note="T -> I (in dbSNP:rs2280962)"
FT /id="VAR_038520"
FT VARIANT 664
FT /note="R -> C (found in a patient with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs138927483)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085490"
FT VARIANT 686
FT /note="R -> C (found in patients with spermatogenic
FT failure; unknown pathological significance;
FT dbSNP:rs376298923)"
FT /evidence="ECO:0000269|PubMed:33963445"
FT /id="VAR_085491"
FT MUTAGEN 22..25
FT /note="ILNV->AAAA: Impairs SUMO2 interaction. Loss of SUMO2
FT interaction; when associated with 76-A--A-79, 97-A--A-100
FT and 121-A--A-124. Loss of SUMO2-dependent recruitment to
FT DNA-protein cross-links (DPCs); when associated with 76-A--
FT A-79; 97-A--A-100 and 121-A--A-124."
FT /evidence="ECO:0000269|PubMed:30914427"
FT MUTAGEN 76..79
FT /note="VVVI->AAAA: Impairs SUMO2 interaction. Loss of SUMO2
FT interaction; when associated with 22-A--A-25, 97-A--A-100
FT and 121-A--A-124. Loss of SUMO2-dependent recruitment to
FT DNA-protein cross-links (DPCs); when associated with 22-A--
FT A-25; 97-A--A-100 and 121-A--A-124."
FT /evidence="ECO:0000269|PubMed:30914427"
FT MUTAGEN 97..100
FT /note="LLEI->AAAA: Impairs SUMO2 interaction. Loss of SUMO2
FT interaction; when associated with 22-A--A-25, 76-A--A-79
FT and 121-A--A-124. Loss of SUMO2-dependent recruitment to
FT DNA-protein cross-links (DPCs); when associated with 22-A--
FT A-25; 76-A--A-79 and 121-A--A-124."
FT /evidence="ECO:0000269|PubMed:30914427"
FT MUTAGEN 121..124
FT /note="IVIS->AAAA: Impairs SUMO2 interaction. Loss of SUMO2
FT interaction; when associated with 22-A--A-25, 76-A--A-79
FT and 97-A--A-100. Loss of SUMO2-dependent recruitment to
FT DNA-protein cross-links (DPCs); when associated with 22-A--
FT A-25; 76-A--A-79 and 97-A--A-100."
FT /evidence="ECO:0000269|PubMed:30914427"
SQ SEQUENCE 691 AA; 76112 MW; F6B63CBF9A7CE1EA CRC64;
MDGCKKELPR LQEPEEDEDC YILNVQSSSD DTSGSSVARR APKRQASCIL NVQSRSGDTS
GSSVARRAPK RQASSVVVID SDSDEECHTH EEKKAKLLEI NSDDESPECC HVKPAIQEPP
IVISDDDNDD DNGNDLEVPD DNSDDSEAPD DNSDDSEAPD DNSDDSEAPD DNSDDSEAPD
DNSDDSDVPD DNSDDSSDDN SDDSSDDNSD DSDVPDDKSD DSDVPDDSSD DSDVPDDSSD
DSEAPDDSSD DSEAPDDSSD DSEAPDDSSD DSEAPDDSSD DSEASDDSSD DSEASDDSSD
DSEAPDDKSD DSDVPEDKSD DSDVPDDNSD DLEVPVPAED LCNEGQIASD EEELVEAAAA
VSQHDSSDDA GEQDLGENLS KPPSDPEANP EVSERKLPTE EEPAPVVEQS GKRKSKTKTI
VEPPRKRQTK TKNIVEPPRK RQTKTKNIVE PLRKRKAKTK NVSVTPGHKK RGPSKKKPGA
AKVEKRKTRT PKCKVPGCFL QDLEKSKKYS GKNLKRNKDE LVQRIYDLFN RSVCDKKLPE
KLRIGWNNKM VKTAGLCSTG EMWYPKWRRF AKIQIGLKVC DSADRIRDTL IHEMCHAASW
LIDGIHDSHG DAWKYYARKS NRIHPELPRV TRCHNYKINY KVHYECTGCK TRIGCYTKSL
DTSRFICAKC KGSLVMVPLT QKDGTRIVPH V
