ID   UP5_HALAI               Reviewed;         173 AA.
AC   P86728;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Uncharacterized protein 5;
DE   Flags: Precursor;
OS   Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Vetigastropoda; Lepetellida; Haliotoidea; Haliotidae; Haliotis.
OX   NCBI_TaxID=109174;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX   PubMed=19915030; DOI=10.1093/molbev/msp278;
RA   Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA   Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA   Degnan B.M.;
RT   "Parallel evolution of nacre building gene sets in molluscs.";
RL   Mol. Biol. Evol. 27:591-608(2010).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 27-37; 59-65 AND 83-94, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Shell {ECO:0000269|PubMed:21050442};
RX   PubMed=21050442; DOI=10.1186/1477-5956-8-54;
RA   Marie B., Marie A., Jackson D.J., Dubost L., Degnan B.M., Milet C.,
RA   Marin F.;
RT   "Proteomic analysis of the organic matrix of the abalone Haliotis asinina
RT   calcified shell.";
RL   Proteome Sci. 8:54-54(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21050442}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix of
CC       calcified shell layers (at protein level).
CC       {ECO:0000269|PubMed:21050442}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EZ420863; Type=Frameshift; Note=Based on peptide sequences from Ref.2, EST GT274178 provides the correct frame.; Evidence={ECO:0000305};
CC       Sequence=GT275233; Type=Frameshift; Note=Based on peptide sequences from Ref.2, EST GT274178 provides the correct frame.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GT273069; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT274178; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT275213; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GT275233; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; EZ420863; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86728; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   InterPro; IPR022041; Methyltransf_FA.
DR   Pfam; PF12248; Methyltransf_FA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..173
FT                   /note="Uncharacterized protein 5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000399451"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        156
FT                   /note="P -> H (in Ref. 1; GT275213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   173 AA;  19652 MW;  6DE6C037A0CABBB4 CRC64;
     MWYKVLGIVS LCSVYVSTQG SNLQCKIAGG GELIPIRTPE YRAWVPLGEV GLNVSDSKVL
     IFAARSCFGA HILLQNNAED FKNAVYEIVI GGMKNTRSGI RQCVGCKFDE WVKDKALNCR
     FFNYFWISWC GDEVWVGHGY RPPHNRILRY KYENQPVINA ASVRSESDTY WAL