ID A0A0Q3LUK5_AMAAE Unreviewed; 3262 AA.
AC A0A0Q3LUK5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQK74216.1};
GN ORFNames=AAES_253921 {ECO:0000313|EMBL:KQK74216.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74216.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74216.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74216.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ADIP family.
CC {ECO:0000256|ARBA:ARBA00009291}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK74216.1}.
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DR EMBL; LMAW01003072; KQK74216.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3LUK5; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 2.
DR Gene3D; 2.20.50.20; Lipovitellin. Chain A, domain 3; 2.
DR Gene3D; 2.20.90.10; Vitellinogen, beta-sheet shell domain; 2.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 2.
DR InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015258; Vitellinogen_b-sht_shell.
DR InterPro; IPR037088; Vitellinogen_b-sht_shell_sf.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR23345:SF15; VITELLOGENIN-1-RELATED; 1.
DR PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR Pfam; PF11559; ADIP; 1.
DR Pfam; PF09175; Vit_b-sht_shell; 2.
DR Pfam; PF09172; Vit_open_b-sht; 2.
DR Pfam; PF01347; Vitellogenin_N; 2.
DR Pfam; PF00094; VWD; 2.
DR SMART; SM01169; DUF1943; 2.
DR SMART; SM01170; DUF1944; 2.
DR SMART; SM00638; LPD_N; 2.
DR SMART; SM00216; VWD; 2.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 2.
DR PROSITE; PS51211; VITELLOGENIN; 2.
DR PROSITE; PS51233; VWFD; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00557}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT DOMAIN 491..1129
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1835..2012
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1947..2610
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 3107..3262
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2869..2903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..129
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 171..198
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 285..312
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 629..655
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
FT DISULFID 2110..2136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
FT DISULFID 2152..2155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 3262 AA; 366551 MW; E941EE91208F8194 CRC64;
MHGFFSAFCT EENIEQSISY LDRELTTLGF PSIYAESKGK ELNLISIINC MNELLVLQHK
NLRAQEEVEM QHLKLGSDMD HLQNCYAKLK VQKLQNIISS RATQYNHDMK RKERXYNKLK
ERLHQLVMNK KDKKIAMEVL NYVGRADGKR GAWRTDKTEA RNEEEMYKVL LSDYEQRQKQ
LLVENAELKK VLQQMKKEII SLLPPQKQKP KERSEDGPVL SDLEEDIGEL NKENMWELSC
ETVREQLTNS IRKQWRXLKN HVEKLDNQVS RVHSGALNEK DVISREDHEM ETEKLELEIQ
QCKEMIKTQQ QLLQQQLMCP CDDDTTVLLQ DCYLLEERER LQEEWRLFRE QRKNFEKERR
SFTEAAIRLG LEVICSVLVV KLASSDQDSR LLKSTSQQRK PRCMLGGPVS AEPCQISQYI
AHNSPVPVKK ENMPSFLIVL YAVMRKLFKS EATAHNVTTK FFVCEDMEGI FYFHPFHYPP
GSQKVDIEPG FSSRKSHWYS YEGWVLNGLQ EKGLAKAGVR LSSKLEISGX SESTYLLKIR
SPQFEEYNGI WPRDPFTRSS KITQIVSSCF SRPFKFEYDS GRIGNIYGPE DCPNMCINIV
RGILNMIQIT IKKSQNVYEL QEAGIGGVCH TRYIIQEDRK NGRVSVTKTV DQNNCQEKVT
KSVGMAYIYP CPVDMMKARL IKGTAAFSYK LKQSESGTLI TEVVSQQVYQ ISPFNEPTGV
AVMEARQQLT LLEVRSERGS TPDISMQSYG GLRYDFSSAL PQMPLQLIKM KNPEQRVVET
LQHIVQNNQQ DFHDDVPYRF LELVQLCRIA STDTLESIWK QFSDKPRYRR WLLSAVSATG
TAEALKFIKT RIRNDDLNYI QTLLSVSFAL HLMKADENTI PIAADLITSS RIQKSPMLQQ
VACLGYSSVV NKYCSQASSC PKEVLQPIHD LADEAISKGR EDKMKLALKC IGNMGEPASI
KRIQKFLPIS ASSASDIPIH IQIDAIMALR KIAWKDPKTV QGHLIQILAD QSLPPEVRVM
ACAIIFETRP ALPLITTIAN VAMKESNLQV ASFVYSHMKA LSKSRLPYLY NISSACNIAL
KLLAPKLDRL SYRYSKVVRI GGYFDNYKVG AAGDVFVMNS AGTMFPSAII SKLTXYSAGS
VADLVEAGVR VEGLTDVITK RNIPFAEYPA YKKIKEIGKA LLGWKELPTE TPLISAYLKL
FGQELAYVNI NKEVLHQVLK AVLEPADRNT AIKKIASQIR SGIAGQWTQP VWFGELRYIV
PTCTGLPLEY GSYTAALARA AASVDGKITP PLTGDFRPSQ LLESTVQIRA DVSPSLYVHT
VATMGVNTEY FQHAVEIQGK VLARVPIKFD AKIDVKQENI KXETNPCXEE TEIVAGSFTL
AYGMLPVVFT YSSPTQQEAD SMPRKHAYSS QEDLRHGIGR KTHKQDICXK LYRLGCQLCF
SRRSRDASFL KNTYLHRLIG EHEAKIVLLP VRTDADIDKI QLEIQAGSRA ASKIIHEVNS
DSEEEDESSP YEDIKAKLKK ILGIEKVFKV ANKTRHQKKQ PSKKGNTMLT ELETDPKAKK
PSSSSSASST VSSSSSSAAS PDRKKAVDED ENDEFPKTKL TAERLSSTYA STRSTHASSR
TASWPKFLGD VKTPVLAVFL HXIRNXEKIG GLQLVVYADI DSVRPRLQVF VSNLTDSTKW
KLCADASVLN AHKAVAYLKW GRNCQDYKIS TELVTGRFAA HPAAQVKVEW PKVPSSVRSI
AEWFYKFVPG AAFMLGFSEK ADKNPSRQAR VIVALTSPRT CDVVVKLPDM ILYEKAXRLP
LSLPVGPRIP ASELQPPIWD VFAEAPSAVL ENLKARCSVS HNKITTFNEV RFNXTMPANC
YHILAQDCSA DLKFLVMMRN VEEAVDLKAI NIKLGSHEID MHPVRGQVXL LVDGVESPTX
NVSYASAGAP LWIYSENQWL VLVAPAYGID KLYFDGYTFR IQVALWMAGK TCGICGKYDA
ECEEEYRMPN GYLAKDAVSF GHSWVLEEKP CTGGYILWRK VKRERASSVA FSMKGLILAL
VLTLVGAQKQ DLEPIFHTGK TYLYSYESFI LHGLPNKGMA MAGVKFTCKV EISHVSHRDH
LLQAGIEGIC QTRYIIQDDS KNNRATIYKS KDLTDCQEKA VKNIGMSYIR PCPTCPLKIR
NMKGTVTFTY KMKYDDTGTS LTSATSQQVY QISPFNERNG ATAMEARQEL SLVSIKRTPL
SAPKIQLQNQ GSLRYHFSGE LLQMPIPLIR IKNPDLQLTE TLRQLVQNNE EGATKEASAK
FLQMIQLFRI VTFDQIESLW MLFGSNPPYR HWFLSAICAA GATDTFRFLK QKVHDEELNI
WEVAVTLPLA FHFVSTNKQT LEIASTFLTC PQIQKLPMHR VIVYLGYGSM VNKYCAQTLV
CPDESLQPLH DLATEATSKG DAKDMALALK AIGNAGEPAS IKRILKFLPT FSQAAVSLPS
RIHADAVLAL RKIARKAPAK VREITLQVFM DNTLAPNVRM VACIVLFETK PALPTVTAMA
SSLLTEPSLQ VASFTYSHMK ALAVGRIPQL YNLSASCNIA IKLLSPRLDR LSYRYSKVFH
VGDYSSKYQA GAIWRVYLMN SPNSMFPSDI ITKVRGYYAN TATDIIEVTL RSQGLTKLIS
NQNIPFAEYD THKTLKELGK TLLGWTELPP ENPLVSAYIK ILGQEIAFVD IDKNAIEQTM
TSLTGSSNWQ VVVKKVVEEV QRGISARWTL PLMVGELRHI VPTVMGVPLE LSLCGAALXQ
AVADVDIRIL PQLSDDFRPS QLXETNMDIH ADIKPKAYFY MIAMMGINTQ YFQSGLEFHA
EFSANTTMKF DARINMKENN LKIETLPCHQ NVELAAVRSE VFAISRNTEE DSEKKSQILP
EGXLPSISNQ PFQPPEKSPR PSSWKLWEVH TDADIDKIQL EIQAGSKAAS KIIDVASSGS
KEEDETTPYK DIQAKLKKIL GIENVFKGFL KWGKDCQDYR LATHIATGQF ATYPAMQMKL
EWPKVPSTVR TTARWFYSFL PGAAYVLGYS QRQQYSPSHQ ATLVMALTSP RTCSVILKLP
ELTIYDRDIR LPLSFPSSPD TSIATPXSPD QNVFIQATIL ITENLKARCS VFQNVITTFN
GVKFNYSMPA NCYHVLAQDC XSELKFLVMM KRLEESSDLT AXNVRLASQL RSQPGRAEEA
RPEIRGSREH GFGSYSVFLP AAVLPGVRPR STGSSRFWGS VSAPTACGPA ARHDKALPSS
GDRSSLVLLE IVTVILDTLR RV
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