ID G3RWY1_GORGO Unreviewed; 4566 AA.
AC G3RWY1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Apolipoprotein B {ECO:0000313|Ensembl:ENSGGOP00000020316.2};
GN Name=APOB {ECO:0000313|Ensembl:ENSGGOP00000020316.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000020316.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000020316.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000020316.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000020316.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Lipid
CC droplet {ECO:0000256|ARBA:ARBA00004502}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR EMBL; CABD030014007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000020316; -.
DR Ensembl; ENSGGOT00000028773.2; ENSGGOP00000020316.2; ENSGGOG00000005179.3.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00590000083139; -.
DR HOGENOM; CLU_000127_0_0_1; -.
DR InParanoid; G3RWY1; -.
DR OMA; FTCAYEN; -.
DR TreeFam; TF331316; -.
DR Proteomes; UP000001519; Chromosome 2A.
DR Bgee; ENSGGOG00000005179; Expressed in liver and 2 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034362; C:low-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034359; C:mature chylomicron; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0035473; F:lipase binding; IEA:Ensembl.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
DR GO; GO:0042953; P:lipoprotein transport; IBA:GO_Central.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0006642; P:triglyceride mobilization; IBA:GO_Central.
DR Gene3D; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 1.
DR Gene3D; 2.20.50.20; Lipovitellin. Chain A, domain 3; 1.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1.
DR InterPro; IPR022176; ApoB100_C.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR009454; Lipid_transpt_open_b-sht.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR PANTHER; PTHR13769; APOLIPOPROTEIN B; 1.
DR PANTHER; PTHR13769:SF1; APOLIPOPROTEIN B-100; 1.
DR Pfam; PF12491; ApoB100_C; 1.
DR Pfam; PF06448; DUF1081; 1.
DR Pfam; PF09172; Vit_open_b-sht; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00557};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..4566
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014125872"
FT DOMAIN 49..675
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT COILED 4363..4390
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 189..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 4566 AA; 516048 MW; B9E5F139CDF03AF8 CRC64;
MGPPRSALLA LLALPALLLL LAGARAGECS YFCYVADVFL PTLGDATRFK HLRKYTYNYE
AESSSGVPGT ADSRSATRIN CKVELEVPQP CSFILKTSQC TLKEVYGFNP EGKALLKKTK
NSEEFAAAMS RYELKLAIPE GKRVFLYPEK DEPTYILNIK RGIISALLVP PETEEAEQVL
FLDTVYGNCS THFTVKTRKS NVATEISTER DLGQCDRFKP IRTGISPLAL IKGMTRPLST
LISSSQSCQY TLDAKRKHVA EAICKEQHLF LPFSYKNKYG MVAQVTQTLK LEDTPKINSR
FFGEGTKKMG LAFESTKSTS PPKQAEAVLK TLQELKKLTI SEQNTQRANL FNKLVTELRG
LSDEAVTSLL PQLIEVSSPI TLQALVQCGQ PQCSTHILQW LKRVHANPLL IDVVTYLVAL
IPEPSAQQLR EIFNMARDQR SRATLYALSH AVNNYHKTNP TGTQELLDIA NYLMEQIQDD
CTGDEDYTYL ILRVIGNMGQ TMEQLTPELK SSILKCVQST KPSLMIQKAA IQALRKMEPK
DKDQEVLLQT FLGDASPGDK RLAAYLMLMR SPSQADINKI VQLLPWEQNE QVKNFVASHI
ANILNSEELD IQDLKKLVKE ALKESQLPTV MDFRKFSRNY QLYKSVSLPS LDPASAKIEG
NLIFDPNNYL PKESMLKTTL TAFGFASADL IEIGLEGKGF EPTLEALFGK QGFFPDSVNK
ALYWVNGQVP DGVSKVLVDH FGYTKDDKRE QDMVNGMMLS VEKLIKDLKS KEVPEARAYL
RILGEELGFA RLHDLQLLGK LLLMGARTLQ GIPQMIGEVI RKGSKNDFFL HYIFMENAFE
LPTGAGLQLQ ISSSGVIAPG AKAGVKLEVA NMQAELVAKP SVSVEFVTNM GIIIPDFARS
GVQMNTNFFH ESGLEAHVAL KAGQLKFIIP SPKRPVKLLS GGNTLHLVST TKTEVIPPLI
ENRQSWSVCK QVFPGLNYCT SGAYSNASST DSASYYPLTG DSRLELELRP TGEIEQYSVS
ATYELQREDR ALVDTLKFVT QAEGAKQTEA TMTFKYNRQS MTLSSEVQIP DFDVDLGTIL
RVNDESTEGK TSYRLTLDIQ NKKITEVALM GHLSCDTKEE RKIKGVISIP RLQAEARSEI
LAHWSPAKLL LQMDSSATAY GSTVSKRVAW HYDEEKIELE WNTGTNVDTK KMTSNFPVDL
SDYPKSLHMY ANRLLDHSVP QTDMTFRHVG SKLIVAMSSW LQKASGSLPY TQTLQDHLNS
LKEFNLQNMG LPDFHIPENL FLKSDGRVKY TLNKNSLKIE IPLPFGGKSS RDLKMLETVR
TPALHFKSVG FHLPSREFQV PTFTIPKLYQ LQVPLLGVLD LSTNVYSNLY NWSASYSGGN
TSTDHFSLRA RYHMKADSVV DLLSYNVQGS GETTYDHKNT FTLSCDGSLR HKFLDSNIKF
SHVEKLGNNP VSKGLLIFDA SSSWGPQMSA SVHLDSKKKQ HLFVKEVKID GQFRVSSFYA
KGTYGLSCQR DPNTGRLNGE SNLRFNSSYL QGTNQITGRY EDGTLSLTST SDLQSGIIKN
TASLKYENYE LTLKSDTNGK YKNFATSNKM DMTFSKQNAL LRSEYQADYE SLRFFSLLSG
SLNSHGLELN ADILGTDKIN SGAHKATLRI GQDGISTSAT TNLKYSLLVL ENELNAELGL
SGASMKLTTN GRFKEHNAKF SLDGKAALTE LSLGSAYQAM ILGVDSKNIF NFKISQEGLK
LSNDMMGSYA EMKFDHTNNL NIAGLTLDFS SKLDNIYSSD KFYKQTVNLQ LQPYSLVTTL
NSDLKYNALD LTNNGKLRLE PLKLHVAGNL KGAYQNNEIK HIYAISSAAL SASYKADTVA
KVQGVEFSHR LNTDIAGLAS AIDMSTNYNS DSLHFSNVFR SVMAPFTMTI DAHTNGNGKL
ALWGEHTGQL YSKFLLKAEP LAFTFSHDYK GSTNHHLVSR KSISAALEHK VSALLTPAEQ
TGTWKLKTQF NNNEYSQDLD AYNTKDKIGV ELTGRTLADL TLLDSPIKVP LLLSEPINII
DALEMRDAIE KPQEFTIVAF VKYDKNQDVH SINLPFFETL QEYFERNRQT IIVVLENVQR
DLKHINIDQF VRKYRAALGK LPQQANDYLN SFNWERQVSR AKEKLTALTK KYRITENDIQ
IALDDAKINF NEKLSQLQTY MIQFDQYIKD NYDLHDLKIA IANIIDEIIE KLKSLDEHYH
IRVNLVKTIH DLHLFIENIH FNKSGSSTAS WIQNVDTKYQ IRIQIQEKLQ QLKRHIQNID
IQHLAGKLKQ HVEAIDVTVL LDQSGTTISF ERINDVLEHV KHFVINLIGD FEVAEKINAF
RAKVHELIER YEVDQQIQVL MDKLVELAHQ YKLKETIQKL SNVLQKVKIK DYFEKLVGFI
DDAVKKLNEL SFKTFIEDVN KFLDMLIKKL KSFDYHQFVD ETNDKIREVT QRLNGEIQAL
ELPQKAEALK LFLEETKATV EVYLESLQDT KITLIINWLQ EALSSASLAH MKAKFRETLE
DTRDRMYQMD IQQELQRYLS LVGQVYSTLV TYISDWWTLA AKNLTDFAEQ YSIQDWAKRV
KALVEQGFTV PEIKTILGTM PAFEVSLQAL QKATFQTPDF IVPLTDLRIP SVQIHFKDLK
NIKIPSRFST PEFTILNTFH IPSFTIDFVE MKVKIIRTID QMLNSELQWP VPDVYLRDLK
VEDIPLARIT LPDFHLPEIA IPEFIIPTLN LNDFQVPDLH IPEFQLPHIS HTIEVPTFGK
LYSILKIQSP LFTLDANADI RNGTTSANEA GIAASITAKG ESKLEVLNFD FQANAQLSNP
KINPLALKES VKFSSKYLRT EHGSEMLFFG NAIEGKSSTV ASLHTEKNTL ELSNGVIVKI
NNQLTLDSNT KYFHKLNIPK LDFSSQADLR NEIKTLLEAG HIAWTSSGKG SWKWACPRFS
DEGTHESQIS FTIEGPLTSF GLSNKINSKH LRVSQNLVYE SGSLNFSKLE IQSQVDSQHV
GHSVLTAKGT ALFGEGKAEF TGRHDAHLNG KVIGTLKNSL FFSAQPFEIT ASTNNEGNLK
VSFPLRLTGK IDFLNNYALF LSPSAQQASW QVSARFNQYK YNQNFSAGNN ENIMEAHVGI
NGEANLDFLN IPLTIPEMHL PYTIITTPPL KDFSLWEKTG LKEFLKTTKQ SFDLSVKAQY
KKNKHRHSIT NPLAVLYEFT SQSIKPFDRH FEKNRNNALD FVTKSYNETK IKFDKYKAEK
SHDELPRTFQ IPGYTVPVVN VEVSPFTIEM SAFGYVFPKA VSMPSFTILG SDIRVPSYTL
ILPSLELPVL HVPRNLKLSL PDFKELYTIS HIFIPAMGNI TYDFSFKSSV ITLNTNAELF
NQSDIVAHLL SSSSSVIDAL QYKLEGTTRL TRKRGLKLAT ALSLSNKFVE GSHNSTVSLT
TKYMEASVAT TAKAQIPILR MNFKQELNGN TKAKPTVSSS MEFKYDFNSS MLYSTAKGAV
DHKLSLESLT SYFSIESSTK GDVKGSVLSR EYSGTIASEA NTYLNSKSTR SSVKLQGTSK
IDDIWNLEVK ENFAGEATLQ RIYSLWEHST KNHLQLEGLF FTNGEHTSKA TLELSPWEMS
ALVQVHASQP SSFHDFPHLG QEVALNANTK NQKIRWKNEV RIHSGSFQSH VELSNDQEKA
HLDIAGSLEG HLRFLKNIIL PVYDKSLWDF LKLDVTTSIG RRQRLRVSTA FVYTKNPNGY
SFSIPVKVLA DKFIIPGLKL NDLNSVLVMP TFHVPFTDLQ VPSYKLDFRE IKIYKKLRTS
SFALNLPTLP EVKFPEVDVL TKYSQSEDSL IPFFEITVPE SQLTVSQFTL PKSVSDGIAA
LDLNAVANKI ADFELPTIIM PEQTIEIPSI KFSVPAGIVI PSFQALTAHF EVDSPLYNAT
WSASLKNKAD CVETVLDSTC SSTVQFLEYE LNVVGTHKIE DGMLASKTKG TFAHRDFSAE
YEEDGKYEGL QEWEGKAYLN IKSPAFTDLH LRYQKDKKGI STSAASPAIG TVGMDMDEDD
DFSKWNFYYS PQSSPDKKLT IFKTELRVRE SDEEIQIKVN WEEEAASGLL TSLKDNVPKA
TGALYDYVNK YHWEHTGLTL REASSKLRRN LQNNAEWVYQ GAIRQIDDID VRFQKAASGT
TGTYQEWKDK AQNLYQELLT QEGQANFQGL KDKVFDGLVR VTQEFHMKVK HLIDSLIDFL
NFPRFQFPGK PGIYTREELC TMFIREVGTV LSQVYSKVHN GSEILFSYFQ DLVITLPFEL
RKHKLIEVIS MYRELLKDLS KEAQEVFKAI QSLKTTEVLR NLQELLQFIF QLIEDNIKQL
KEMKFTYLIN YIQDEINTIF NDYIPYVFKL LKENLCLNLH KFNEFIQNEL QEASQELQQI
HQYIMALREE YFDPSIVGWT VKYYELEEKI VSLIKNLLVS LKDFHSEYIV SASDFTSQLS
SQVEQFLHRN ILEYLSILTD PDGKGKEKIA ELSATAQEII KSQAIATKKI ISDYHQQFRY
KLQDFSDQLS DYYEKFIAES KRLIDLSIQN YHTFLIYIKE LLKKLQSTTV MNPYMKLAPG
ELTIIL
//