MYP_STRPU
ID MYP_STRPU Reviewed; 1357 AA.
AC P19615; Q8T3T2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Major yolk protein;
DE Short=MYP;
DE AltName: Full=Vitellogenin;
DE Flags: Precursor;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IRON-BINDING.
RX PubMed=11969251; DOI=10.1006/dbio.2002.0611;
RA Brooks J.M., Wessel G.M.;
RT "The major yolk protein in sea urchins is a transferrin-like, iron binding
RT protein.";
RL Dev. Biol. 245:1-12(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-137.
RX PubMed=2827123; DOI=10.1093/nar/15.24.10405;
RA Shyu A.B., Blumenthal T., Raff R.A.;
RT "A single gene encoding vitellogenin in the sea urchin Strongylocentrotus
RT purpuratus: sequence at the 5' end.";
RL Nucleic Acids Res. 15:10405-10417(1987).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=3520559; DOI=10.1073/pnas.83.11.3865;
RA Shyu A.B., Raff R.A., Blumenthal T.;
RT "Expression of the vitellogenin gene in female and male sea urchin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3865-3869(1986).
CC -!- FUNCTION: May serve the following two functions: a classical role as a
CC yolk protein precursor and probably shuttle iron to developing germ
CC cells.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in the intestines of the females and
CC males and also in ovaries and testis. {ECO:0000269|PubMed:3520559}.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68565.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY090112; AAM14717.1; -; mRNA.
DR EMBL; Y00513; CAA68565.1; ALT_FRAME; Genomic_DNA.
DR PIR; S00696; S00696.
DR RefSeq; NP_999740.1; NM_214575.1.
DR AlphaFoldDB; P19615; -.
DR STRING; 7668.SPU_013301-tr; -.
DR Allergome; 8814; Str pu Vitellogenin.
DR PRIDE; P19615; -.
DR EnsemblMetazoa; NM_214575; NP_999740; GeneID_373376.
DR GeneID; 373376; -.
DR KEGG; spu:373376; -.
DR CTD; 446200; -.
DR eggNOG; ENOG502QRSZ; Eukaryota.
DR HOGENOM; CLU_257895_0_0_1; -.
DR OMA; RKEWACA; -.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; P19615; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR Pfam; PF00405; Transferrin; 2.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 1.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Storage protein; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1357
FT /note="Major yolk protein"
FT /id="PRO_0000035750"
FT DOMAIN 132..478
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 493..1101
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1081
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 85
FT /note="E -> V (in Ref. 2; CAA68565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1357 AA; 154019 MW; A41BD91F76C92F73 CRC64;
MRAAILFCLV ASSMAVPSGS LGSRPGTCPP QPSDQVMIEA TRCSYVYGLT WDWNCNSQGQ
ENYKCCQYEN DIRICVPPIP ADVDEEVGVE QPSQSVDQVR QAIQKTQDFI RKVGLYPAPD
QRRRTTPTPD TVRWCVSSRC QMTKCQRMVS EFTYSPNMVP RKQWKCTQAT SQEQCMFWIE
QGWADIMTTR EGQVYSANTT FNLKPIAYET TINDQQPEIQ ILKHYQNVTF ALKSSRLVNP
NTFSELRDKT TCHAGIDMPD FDMPASFADP VCNLIKEGVI PVTGNYIESF SDFVQESCVP
GVLNMTYNKN GTYPLSLVTL CEDQQYKYSG IKGALSCLES GKGQVTFVDQ KVIKKIMSDP
NVRDNFQVVC RDESRPLDEE IFTDVTCHVG HTARPTIFIN KNNTQQKETD IKTLVVKMME
LYGNTDRDVN FNIFDSSVYD CGKCQMTGKP LNKNLIFLEE SNTMKIVDDS KVYAGEVYAA
YNVCSKLVPK PRAKICVTNV TEYEACRRFK GIAENIPEVK KVAWGCVLAN SSIECMQAVH
NNTADLFKAN PMETFIAGKE FLLDPLMSVH RNDSVTMNHT YTRTLAVIKR SSLAKFPGLL
SVPEGQPKYI KDLWKLKICS AGLKNFSAFH SPIGYLLANG TIPRIGSVFE SVNRYFQATC
VPEIEPETWR LDSDLLLGRE MNWGFSSLNM YNFTGQEWLL WNTPATWNFL TYNRKVSTGL
DIKKLIELKK QNLTSHIFNQ NLSSPRNVEL LDDLVGVEGI SDLVKGVQDT IGPEGKQKMN
MLRDRLSNSF PNFEAVRTLS DKVDIVNKMK DARQQRLQNK DHPFGNVIQE TFQGHLMVDV
FSKLLELRSD KISTLEEIIS HVKTIPYLTD FKDVEITTVL KHPAIMSYVE IYFPRLSQTF
VEPFDNVELR EREFNRYTNP LWLSPKVHTY LDLVKNHQTE ITKTCNSNLP LNFKGYEGAL
RCLKSGVADL ASSTSRPSVT RTLRDTDLST GWVHLQRPPP SLPQRQVVEI DVNMDIAKVC
NFGEVMNPVL VTAYNTSGSW RWNITKALMI AHQSVALPAL FGEGTVMGKD YDMLLPIAPL
NQSYQPFLGS KPLRSMEAIV KASSYDWFKD QTGICYGETY TNIVKQRNET CQAIVKDVTC
VGTPRMKKIS VGRFGAKQFK MIKMCSRPSK FVRKMADFQC DNGFGYLKPV ITAVACECML
CEEMIEYNTS FTEDNMWSDV SNKYVLTGEQ DIYRQIPIWG NNSYFYDHTL NKNFELGNHS
IIVEHVQTVV VERPSPGILS QVNSEVDPEV QVQMDSASLT KTCETVWNGQ SWLPERFQGY
KTSGSCVVPE TGANAKSRVD RFRQIMQRKQ QLVDHHH
