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Database: UniProt
Entry: U3K520_FICAL
LinkDB: U3K520_FICAL
Original site: U3K520_FICAL 
ID   U3K520_FICAL            Unreviewed;      1760 AA.
AC   U3K520;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Tubulin gamma complex associated protein 6 {ECO:0000313|Ensembl:ENSFALP00000010124.2};
GN   Name=TUBGCP6 {ECO:0000313|Ensembl:ENSFALP00000010124.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000010124.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000010124.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000010124.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
CC   -!- SIMILARITY: Belongs to the TUBGCP family.
CC       {ECO:0000256|ARBA:ARBA00010337}.
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DR   STRING; 59894.ENSFALP00000010124; -.
DR   Ensembl; ENSFALT00000010164.2; ENSFALP00000010124.2; ENSFALG00000009698.2.
DR   eggNOG; KOG2000; Eukaryota.
DR   GeneTree; ENSGT00940000157810; -.
DR   HOGENOM; CLU_002518_0_0_1; -.
DR   Proteomes; UP000016665; Chromosome 1A.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000931; C:gamma-tubulin ring complex; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0007020; P:microtubule nucleation; IEA:Ensembl.
DR   Gene3D; 1.20.120.1900; Gamma-tubulin complex, C-terminal domain; 1.
DR   InterPro; IPR007259; GCP.
DR   InterPro; IPR045818; GCP6_N.
DR   InterPro; IPR040457; GCP_C.
DR   InterPro; IPR042241; GCP_C_sf.
DR   InterPro; IPR041470; GCP_N.
DR   PANTHER; PTHR19302; GAMMA TUBULIN COMPLEX PROTEIN; 1.
DR   PANTHER; PTHR19302:SF70; GAMMA-TUBULIN COMPLEX COMPONENT 6; 1.
DR   Pfam; PF19340; GCP6_N; 1.
DR   Pfam; PF04130; GCP_C_terminal; 1.
DR   Pfam; PF17681; GCP_N_terminal; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        444..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        474..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..344
FT                   /note="Gamma-tubulin complex component 6 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19340"
FT   DOMAIN          355..617
FT                   /note="Gamma tubulin complex component protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17681"
FT   DOMAIN          1436..1719
FT                   /note="Gamma tubulin complex component C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04130"
FT   REGION          258..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1176..1332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1258..1279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1760 AA;  199995 MW;  A846EAFBDB3CDBDD CRC64;
     MESITQLFSD LCEAHLTGLP WKVHLGRQKI SKRRAKQNLK RIAYNALFMN LFQDEARKLQ
     SNVSRLPVKN KILMLSFNLR VAGLGAQADR LENLVEELET AECLPFTEVN SVLDLLVQLA
     GTGPPQLVPQ KKDYFLNNKY VGRNVKYQGY DYYDVSVFEA DIQSLITNEE CQFNDTIQQT
     LQIMEAAPGT GLPAIGLFSQ SCPAGDKFEK ETRVSLFGAL VHSRTYDMDI KLDLPPVPDN
     ADLSGLAIKV PQSIDQSEDE GFQSASNLTP DSQSEPSITP DIDLWDAVLT YGPSKRRCWE
     RIGYPPGKKE EPYLTEAGRE AFDKFYKLRE GELQLFTNTV LQLPQLVLVK EPELVKDVLN
     VLIGVVSTTF SLNQAAQSFV IREGVYVSGT SPETMHNLLS EVAEYGTYYT RLSRFSLQPV
     LDSSYSKGLV FQAFTSGLRK YLQYYRACVL STPPTLSLLT ISFLFRKLGR QLRYLAELCG
     IGTTALVISG GAGASFPTGV KLLSYLYKEA LNNCSNEHYP VLLSLLKTSC EPYTRFIYDW
     VYSGVFRDVY GEFMIQVNED YLCFRDKHYW THGYVLISKE VEDCVPVFLK HIANDVYICG
     KTINLLKLCC PRHYICWSDI PVPRISVIFS LEELKEIERD CAVYVGRMER IARYSSISKE
     EKDLRMEIAK QELIVHARET ASKVLKAISD KQISERMALD AKKREQFQKL KEQFAKDQER
     RLAIKQEEID DDFSYARELR EREKRLKALE EELEKKARQE LIDHYSKLSD DAARREQRTL
     WKIQRHKLET ARLKFLLEDQ KRIEEMLEKL PDGNYRRKLD IIPYKECQLA LDKNPVEKDP
     PSQVSFVKPL HSNETVGRKE PEPEQGYAAS ADKALPTAEP ENNNADEHFQ PKATGSESNL
     QNSEEACSAE PLPESNVNIE DFLSKSQDEQ SIAVRVQGSL LDEAFQNINS DLSETLQVSE
     SQPVLRGAPE EDNAPLHQQS EYDFNTVLRP SAAWQGHVGV GENVFDVDNR RPRWNIHGHA
     SDSNIRVGEY VPQVDAYQPH PSPHGHSSDS HIKSSSYTSE VEPRRPRWNI HGHVSEAHIK
     IGEYASETAT SRPRWNVHGH ASEANIKIGE YVSNVAPTRP RWSSHGHASD ANIKIGENVS
     EVVSARPRWN IHGHASQSHI KIGELVSDTE PVKSRWSPFG HASQSSIQIG KWAPSVENDP
     IPHRKTISGS SSDSTVQTLL YSEELPPAEG SRKEAEPSQV KEETLPPSQI SDSVTDFPDA
     NIKDDKKENS KEKNQEVIAD VVNKDPSPDS SQNLQREEPE KAVPQDTVPQ ETLSSEANAP
     TTKEEDGEEE DTWKKEQAYL KALSDQYCIE KYQDSYDLMS EPPVSHLLHH VIPRSYTFPV
     DPMVQSATDE TAVQLSELLS LPVLMKRSIT APLVSHVSLV NKAIVDYYFV ELNVEKHFEA
     LRHFLLMEDG EFAQSLSDLL FEKLGSGQTP GELLNPLVLN SILNKALQYS LHGDTQLASN
     LSFALKYLPE MFKPNAPDVL SCLELRYKVD WPLNIVITES CMNKYNKIFS FLLQLKHMVW
     TLKDVWFHLK RTALVSSASN SVQFRQLQLY KHEMQHFVKV IQGYIANQIL HVTWCEFGNK
     LSSVGNLEEI HRTHAEYLNK AIFRGLLTEK AAPVMNIIHS IFSLILKFRS QLISQSWSFD
     AGKQMAVHPN FGLMQQSYNT FKYYSHFLFK GCPKMVSKDQ KQIFQDELEW LLPNSTGNQN
     TCGSHLSPYY EIYACFMDRD
//
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