ID L5KSJ9_PTEAL Unreviewed; 2562 AA.
AC L5KSJ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glycine cleavage system H protein, mitochondrial {ECO:0000256|ARBA:ARBA00018130};
DE AltName: Full=Lipoic acid-containing protein {ECO:0000256|ARBA:ARBA00033419};
GN ORFNames=PAL_GLEAN10016154 {ECO:0000313|EMBL:ELK14434.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK14434.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the GcvH family.
CC {ECO:0000256|ARBA:ARBA00009249}.
CC -!- SIMILARITY: Belongs to the polycystin family.
CC {ECO:0000256|ARBA:ARBA00007200}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; KB030572; ELK14434.1; -; Genomic_DNA.
DR STRING; 9402.L5KSJ9; -.
DR eggNOG; KOG3599; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; L5KSJ9; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd22831; Gal_Rha_Lectin_PKD1L2; 1.
DR CDD; cd06848; GCS_H; 1.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR HAMAP; MF_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR InterPro; IPR046791; Polycystin_dom.
DR InterPro; IPR014010; REJ_dom.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00527; gcvH; 1.
DR PANTHER; PTHR10877:SF134; POLYCYSTIC KIDNEY DISEASE PROTEIN 1-LIKE 2; 1.
DR PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01597; GCV_H; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR Pfam; PF02010; REJ; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2562
FT /note="Glycine cleavage system H protein, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969515"
FT TRANSMEM 1360..1379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1567..1588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1608..1629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1840..1858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1870..1890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1948..1970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2186..2206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2226..2243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2275..2295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2315..2334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2340..2368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..154
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 162..253
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 423..1138
FT /note="REJ"
FT /evidence="ECO:0000259|PROSITE:PS51111"
FT DOMAIN 1404..1521
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 2455..2537
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1639..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2496
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
FT DISULFID 2044..2057
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 2562 AA; 285105 MW; 7B97B4BA2EDB405D CRC64;
MNAASLVLLG LSLRFMATTA RPEEGSFCSK SQVAFRDSCY EFVPLGRSFY GAQNWCERRG
GHLVFIHDEG TQWFLQKHIS QDREWWIGLT GNSAQNGTTE GLGIWLDTSN VNYSHWHGGQ
AAPAPNTCGY IGRDPSSRWA ASDNCTQPFA FICEFGVGQS LACEGLNAIM HCGSGEVIQI
QDAFYGRQTP HYCIQDAGHP SDLEEECSWV SVKDEVAGQC QGLQACQVAA NATFFGDLCP
TQGSYLWVQY QCREGLQLTV SNESFTFDNV TISLTWLLSP YIGNLSCIIS TGDGHTFDPY
YPLSLSSNVI YQFTNPGEFT VLAECTTSEW HVTAQKQVTM RDKMERLSVT GCSGLSKLGG
GFLCWAVFGD PMWIQVELDG GTVVTYTVLL GNTTLAESTT QRGLLPYNLT LDRVAQQWMG
PGMHHLEICA TSSTTTSPLS TNITVHFMEP LSGLRASWAS DHLELGQDLL VNVSVAHGIP
EKLTFEVAGL NASFSHEEES LGWPSGIYHV AVPLEGTFLV TVLVRNAFSN LSLEIGSITV
TGKSYLQGNC SEVKTGMPTV ERYLTNQLLF LQRDKENVEV YLEPGRYVDP FMTVTLGWPD
SDKDLHFQWS CGRCWAQWRD CVERQLLCTD QKKLVVPPSC LPPPNSAVTL RLALWKGQEL
VKQEEQCLYV SASMELKPQV SCVKNCGPVN AGEDIMLRVT MEDDSLVAMF SWYLDDTPLE
KVEPLPEACR LRGFWPRSLT LLHSNTSTLV LNSSLLQTWG QVIRIRVTAV TGHAYGEDTY
MISNLPTPEV PTCTVSPEEG TVLTSFAIFC NASAALGPLE YCFCLESGTC LHCGPDPALP
SVYLPLGKEN NDFVLTVVIS VSNRAGERQQ THAAVKVGLG DAHIEDMAFQ TAVSENIITA
LQGERGPEQL FQLARSVSSM LDQECQGLGS TGPQRMEARK KVREHVLGSL SVVTATLGDM
QRVQGLAKVL REVTHRCEEL TPLAQREAAW VLQHASEALL AVSVKAHPED QRRQAATRDL
FQAVGSVLES SLRDGLEEPE EAHGSQTATV SQLLRAVEHV QAALLLGRLP GGLPATLATP
SISVYTNRIQ PRSWQSSSMH IAPASSATFT LPAASSLGFM EDDQEPVDIR MMSFSKSPFL
AQSHFDVSGT VGGLSLTSPS GQLIPMKNLS ENIEILLPRL SRYSEPTVLN LISPEALWVN
MTLRGMALGI QLHWRPDIPL MLCLGYGYHP NKTSYDAKAH LPPMAVPDGM STWILSPEDL
HFGEGVYYLT VIPESDLEPT PGRDLTVGIT TFLSHCVFWD EGQGTWDNSG CQVGSQTTVS
QTHCLCNHLT FFGSTFLVMP NAIDVRQTGE LFATFEDNPV VVTTVGCLCV AYVLVIIWAR
RKDAQDQAKV KVTVLEDNDP FAQYHYLVTV YTGHRRGAAT SSKVTVTLYG LDGESEPHHL
SDPDIPVFER GGVDVFLLST LFPLGELRSL RLWHDNSGDR PSWYVSRVLV HDLVMDQKWY
FLCNSWLSIN VGDCVLDKVF PVATEQDRKQ FSYLFFMKTS MDFQDGHIWY SIFSRSARSN
FTRVQRVSCC FSLILCTMLT SIMFWGVPKD PAEQKMDLGQ IEFTWQEVMI GLESSLLMFP
INLLIVQIFR NTHPWVTKEQ STGKRDRGSL SPAPTPQPME DGPLTPEVVT KDMWRLVSSL
FKALKVPSPT LGWDSANLMD INQLLALVED VICLQNMAGQ MFQEEAKQRE DPLTLTLGSI
QMKEKMQLLT PEVGPSNPRK DSVYRQCLYL QLEHVEQELR LVGPRGFPQR QSHARALRQL
QTLKGYLAGQ LGTPPPAHIS GVAGFFTMLY GLHYGRASSL KWLISMAVSF VESVFVTQPL
KELMVSNLDL GSTVGIFQVL GFAAFFALVL KRVEDEEEPI VPLLRHLSSP DPSSLFRVRR
NSRKDIYQPP LAANIEKMKT TQLKEQKAFA LIREIFAYLG FLWMLLLVAY GQRDPSAYHF
NRHLQHSFTQ GFSAILSFQE FFTWANTTLI SNLYSHHSGF ITDGNSKLVG SAQVRQVRVR
ESSCLLAPQL QTSLNRCHAP YSLDVEDLSD YGEGWNASNL NSSNGFSQAW QYQSQSQRRG
YPIWGKLTVY QGGGYVVPLG TDHQSASRIL QYLFDNTWLD SLTRAVFVEF TVYNANVNLF
CIITLTLETS ALDLQSLRLY HFTDGWHPFV VAAEVFYLLF LFYYMVVQGK LIWKQKWCYF
HSKWNLLELA IILASWSALA AFVKRTILAE RDIQGYRKRR EEVISLSETA AADAALGYII
AFLVLLSTVK LWHLLRLNPK MNMITSALRR AWGDISGFVI VIFIMLLAYS IAVLDYSPVL
GSFLIGSCII FMTFVVLNLF ISVILVAFNE EQKYYQVTEP GVADLASTFT LRKRRPSHSP
TPPGLRAASA PAAPCAPRFW GLRAGAIRTL RTGPNLLSVR KFTEKHEWIT TENGIGTVGI
SNFAQEALGD VVYCSLPEVG TKLNKQDEFG ALESVKAASE LYSPLSGEVT EINEALAENP
GLVNKSCYDD GWLIKMTLSN PSELDELMSE EAYEKYIKSI EN
//
