VIT_ICHUN
ID VIT_ICHUN Reviewed; 1823 AA.
AC Q91062;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Vitellogenin;
DE Short=VTG;
DE Contains:
DE RecName: Full=Lipovitellin LV-1N;
DE Contains:
DE RecName: Full=Lipovitellin LV-1C;
DE Contains:
DE RecName: Full=Lipovitellin LV-2;
DE Flags: Precursor;
OS Ichthyomyzon unicuspis (Silver lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Ichthyomyzon.
OX NCBI_TaxID=30308;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 708-714 AND 1306-1314.
RC TISSUE=Liver;
RX PubMed=1507234; DOI=10.1016/0022-2836(92)90642-w;
RA Sharrock W.J., Rosenwasser T.A., Gould J., Knott J., Hussey D.,
RA Gordon J.I., Banaszak L.J.;
RT "Sequence of lamprey vitellogenin. Implications for the lipovitellin
RT crystal structure.";
RL J. Mol. Biol. 226:903-907(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 AND 6.0 ANGSTROMS).
RX PubMed=3398048; DOI=10.1016/0022-2836(88)90542-6;
RA Raag R., Appelt K., Xuong N.-H., Banaszak L.J.;
RT "Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin
RT at 2.8-A resolution.";
RL J. Mol. Biol. 200:553-569(1988).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 17-1072 AND 1306-1624, AND
RP PYROGLUTAMATE FORMATION AT GLN-17.
RX PubMed=12135361; DOI=10.1021/bi025674w;
RA Thompson J.R., Banaszak L.J.;
RT "Lipid-protein interactions in lipovitellin.";
RL Biochemistry 41:9398-9409(2002).
CC -!- FUNCTION: Precursor of the major egg-yolk proteins that are sources of
CC nutrients during early development of oviparous organisms.
CC -!- TISSUE SPECIFICITY: Produced by the liver, secreted into the blood and
CC then sequestered by receptor mediated endocytosis into growing oocytes,
CC where it is generally cleaved, giving rise to the respective yolk
CC components lipovitellins 1 and 2.
CC -!- INDUCTION: By steroids (estrogen).
CC -!- PTM: What corresponds to phosvitin in other species is lost during
CC maturation of vitellogenin to lipovitellin.
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DR EMBL; M88749; AAA49327.1; -; mRNA.
DR PIR; S28974; S28974.
DR PDB; 1LSH; X-ray; 1.90 A; A=18-1072, B=1306-1624.
DR PDBsum; 1LSH; -.
DR AlphaFoldDB; Q91062; -.
DR SMR; Q91062; -.
DR PRIDE; Q91062; -.
DR EvolutionaryTrace; Q91062; -.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.20.50.20; -; 2.
DR Gene3D; 2.20.90.10; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
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 Pfam; PF09172; DUF1943; 1.
DR Pfam; PF09175; DUF1944; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM01170; DUF1944; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 3.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Pyrrolidone carboxylic acid; Signal; Storage protein.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..1823
FT /note="Vitellogenin"
FT /id="PRO_0000041572"
FT CHAIN 17..707
FT /note="Lipovitellin LV-1N"
FT /id="PRO_0000041573"
FT CHAIN 708..1074
FT /note="Lipovitellin LV-1C"
FT /id="PRO_0000041574"
FT CHAIN 1306..1624
FT /note="Lipovitellin LV-2"
FT /id="PRO_0000041575"
FT DOMAIN 18..658
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1564..1732
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 953..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:12135361"
FT CARBOHYD 1097
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1566..1695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1589..1731
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 41..56
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 58..80
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 166..185
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 207..221
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 224..238
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 248..263
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 425..443
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 455..466
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 470..483
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 489..493
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 508..516
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 526..538
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 544..556
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 561..571
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 577..590
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 599..609
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 615..618
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 625..633
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 634..637
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 638..649
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 652..666
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 669..679
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 681..687
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 738..745
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 748..756
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 779..789
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 792..810
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 814..836
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 847..850
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 855..876
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 881..903
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 904..907
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 908..913
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 920..935
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 938..945
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 996..1001
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1009..1013
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 1018..1021
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1022..1033
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 1034..1036
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 1040..1043
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1045..1055
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1064..1069
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1360..1366
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1375..1383
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 1385..1387
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1391..1399
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1406..1412
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1415..1429
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1431..1455
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 1460..1471
FT /evidence="ECO:0007829|PDB:1LSH"
FT HELIX 1473..1479
FT /evidence="ECO:0007829|PDB:1LSH"
FT TURN 1480..1482
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1484..1487
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1494..1503
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1506..1512
FT /evidence="ECO:0007829|PDB:1LSH"
FT STRAND 1517..1524
FT /evidence="ECO:0007829|PDB:1LSH"
SQ SEQUENCE 1823 AA; 199945 MW; B29B9C65516C799B CRC64;
MWKLLLVALA FALADAQFQP GKVYRYSYDA FSISGLPEPG VNRAGLSGEM KIEIHGHTHN
QATLKITQVN LKYFLGPWPS DSFYPLTAGY DHFIQQLEVP VRFDYSAGRI GDIYAPPQVT
DTAVNIVRGI LNLFQLSLKK NQQTFELQET GVEGICQTTY VVQEGYRTNE MAVVKTKDLN
NCDHKVYKTM GTAYAERCPT CQKMNKNLRS TAVYNYAIFD EPSGYIIKSA HSEEIQQLSV
FDIKEGNVVI ESRQKLILEG IQSAPAASQA ASLQNRGGLM YKFPSSAITK MSSLFVTKGK
NLESEIHTVL KHLVENNQLS VHEDAPAKFL RLTAFLRNVD AGVLQSIWHK LHQQKDYRRW
ILDAVPAMAT SEALLFLKRT LASEQLTSAE ATQIVYSTLS NQQATRESLS YARELLHTSF
IRNRPILRKT AVLGYGSLVF RYCANTVSCP DELLQPLHDL LSQSSDRADE EEIVLALKAL
GNAGQPNSIK KIQRFLPGQG KSLDEYSTRV QAEAIMALRN IAKRDPRKVQ EIVLPIFLNV
AIKSELRIRS CIVFFESKPS VALVSMVAVR LRREPNLQVA SFVYSQMRSL SRSSNPEFRD
VAAACSVAIK MLGSKLDRLG CRYSKAVHVD TFNARTMAGV SADYFRINSP SGPLPRAVAA
KIRGQGMGYA SDIVEFGLRA EGLQELLYRG SQEQDAYGTA LDRQTLLRSG QARSHVSSIH
DTLRKLSDWK SVPEERPLAS GYVKVHGQEV VFAELDKKMM QRISQLWHSA RSHHAAAQEQ
IRAVVSKLEQ GMDVLLTKGY VVSEVRYMQP VCIGIPMDLN LLVSGVTTNR ANLHASFSQS
LPADMKLADL LATNIELRVA ATTSMSQHAV AIMGLTTDLA KAGMQTHYKT SAGLGVNGKI
EMNARESNFK ASLKPFQQKT VVVLSTMESI VFVRDPSGSR ILPVLPPKMT LDKGLISQQQ
QQPHHQQQPH QHGQDQARAA YQRPWASHEF SPAEQKQIHD IMTARPVMRR KQHCSKSAAL
SSKVCFSARL RNAAFIRNAL LYKITGDYVS KVYVQPTSSK AQIQKVELEL QAGPQAAEKV
IRMVELVAKA SKKSKKNSTI TEEGVGETII SQLKKILSSD KDKDAKKPPG SSSSSSSSSS
SSSSSSSSDK SGKKTPRQGS TVNLAAKRAS KKQRGKDSSS SSSSSSSSSD SSKSPHKHGG
AKRQHAGHGA PHLGPQSHSS SSSSSSSSSS SSASKSFSTV KPPMTRKPRP ARSSSSSSSS
DSSSSSSSSS SSSSSSSSSS SSSSESKSLE WLAVKDVNQS AFYNFKYVPQ RKPQTSRRHT
PASSSSSSSS SSSSSSSSSS SDSDMTVSAE SFEKHSKPKV VIVLRAVRAD GKQQGLQTTL
YYGLTSNGLP KAKIVAVELS DLSVWKLCAK FRLSAHMKAK AAIGWGKNCQ QYRAMLEAST
GNLQSHPAAR VDIKWGRLPS SLQRAKNALL ENKAPVIASK LEMEIMPKKN QKHQVSVILA
AMTPRRMNII VKLPKVTYFQ QGILLPFTFP SPRFWDRPEG SQSDSLPAQI ASAFSGIVQD
PVASACELNE QSLTTFNGAF FNYDMPESCY HVLAQECSSR PPFIVLIKLD SERRISLELQ
LDDKKVKIVS RNDIRVDGEK VPLRRLSQKN QYGFLVLDAG VHLLLKYKDL RVSFNSSSVQ
VWVPSSLKGQ TCGLCGRNDD ELVTEMRMPN LEVAKDFTSF AHSWIAPDET CGGACALSRQ
TVHKESTSVI SGSRENCYST EPIMRCPATC SASRSVPVSV AMHCLPAESE AISLAMSEGR
PFSLSGKSED LVTEMEAHVS CVA
