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Database: UniProt
Entry: H2Q8N4_PANTR
LinkDB: H2Q8N4_PANTR
Original site: H2Q8N4_PANTR 
ID   H2Q8N4_PANTR            Unreviewed;      1299 AA.
AC   H2Q8N4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 5 {ECO:0000256|ARBA:ARBA00041448};
GN   Name=TTLL5 {ECO:0000313|Ensembl:ENSPTRP00000011141.4,
GN   ECO:0000313|VGNC:VGNC:3292};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000011141.4, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000011141.4, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000011141.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-
CC         glutamyl-L-glutamyl-[protein] + H(+) + phosphate;
CC         Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036640};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145;
CC         Evidence={ECO:0000256|ARBA:ARBA00036640};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; AACZ04008411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04008412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04008413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04008414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPTRT00000012032.4; ENSPTRP00000011141.4; ENSPTRG00000006560.6.
DR   VGNC; VGNC:3292; TTLL5.
DR   eggNOG; KOG2157; Eukaryota.
DR   GeneTree; ENSGT00940000162939; -.
DR   HOGENOM; CLU_006704_1_0_1; -.
DR   InParanoid; H2Q8N4; -.
DR   TreeFam; TF313087; -.
DR   Proteomes; UP000002277; Chromosome 14.
DR   Bgee; ENSPTRG00000006560; Expressed in testis and 21 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF145; TUBULIN POLYGLUTAMYLASE TTLL5; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT   REGION          585..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          832..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..617
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1299 AA;  145516 MW;  80D994F62A196122 CRC64;
     MPIVMARDLE ETASSSEDEE VISQEDHPCI MWTGGCRRIP VLVFHADAIL TKDNNIRVIG
     ERYHLSYKIV RTDSRLVRSI LTAHGFHEVH PSSTDYNLMW TGSHLKPFLL RTLSEAQKVN
     HFPRSYELTR KDRLYKNIIR MQHTHGFKAF HILPQTFLLP AEYAEFCNSY SKDRGPWIVK
     PVASSRGRGV YLINNPNQIS LEENILVSRY INNPLLIDDF KFDVRLYVLV TSYDPLVIYL
     YEEGLARFAT VRYDQGAKNI RNQFMHLTNY SVNKKSGDYV SCDDPEVEDY GNKWSMSAML
     RYLKQEGRDT TALMAHVEDL IIKTIISAEL AIATACKTFV PHRSSCFELY GFDVLIDSTL
     KPWLLEVNLS PSLACDAPLD LKIKASMISD MFTVVGFVCQ DPAQRASTRP IYPTFESSRR
     NPFQKPQRCR PLSASDAEMK NLVGSAREKG PGKLVGSVLG LSMEEIKVLR RVKEENDRRG
     GFIRIFPTSE TWEIYGSYLE HKTSMNYMLA TRLFQDRGNP RRSLLTGRTR MTADGAPELK
     IESLNSKAKL HAALYERKLL SLEVRKRRRR SSRLRAMRPK YPVITQPAEM NVKTETESEE
     EEEVSLDNED EDQEASQEES AGFLRENQAK YTPSLTALVE NTPKENSMKV REWNNKDGHC
     CKLETQELEP KFNLMQILQD NGNLSKVQAR IAFSAYLQHV QIRLMKDSGS QTFSASWAAK
     EDEQMELVVR FLKRASNNLQ HSLRMVLPSR RLALLERRRI LAHQLGDFII VYNKETEQMA
     EKKSKKKVEE EEEDGVNTEN FQEFIRQASE AELEEVLTFY TQKNKSASVF LGTHSKSSKN
     NNSYSDSGAK GDHPETIMEE VKIKPPKQQQ TTEIHSDKLS RFTTSAEKEA KLVDSNSSSG
     PTATLQKIPN THLSSVTTSD LSPGPCHHSS LSQIPSAIPS MPHQPTILLN TVSASASPCL
     HPGAQNIPSP AGLPRCRSGS HTIGPFSSFQ SAAHIYSQKL SRPSSAKAAG SCYLNKHHSG
     IAKTQKEGED ASLYSKRYNQ SVVTAELQRL AEKQAARQYS PSSHINLLTQ QVTNLNLATG
     IINRSSASTP PTLRPIISPS GPTWSTQSDP QAPENHSSSP GSRSLQTGGF AWEGEVENNV
     YSKATGVVPQ HKYHPTAGSY QLHFALQQLE QQKLQSRQLL DQSRARHQAI FGSQTLPNSN
     LWTMNNGAGC TISSATASGQ KPTTLPQKVV PPPSSCASLV PKPPPNHKQV LRRATSQKTS
     KGSSAEGQLN GLQSSLNPAA FVPITSSTDP ISTKKNVFN
//
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