SEC63_HUMAN
ID SEC63_HUMAN Reviewed; 760 AA.
AC Q9UGP8; O95380; Q5THN4; Q86VS9; Q8IWL0; Q9NTE0;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Translocation protein SEC63 homolog;
GN Name=SEC63 {ECO:0000303|PubMed:28375157, ECO:0000312|HGNC:HGNC:21082};
GN Synonyms=SEC63L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10543453; DOI=10.1515/bc.1999.142;
RA Skowronek M.H., Rotter M., Haas I.G.;
RT "Molecular characterization of a novel mammalian DnaJ-like Sec63p
RT homolog.";
RL Biol. Chem. 380:1133-1138(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10799540; DOI=10.1074/jbc.275.19.14550;
RA Meyer H.-A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.-U.,
RA Hartmann E.;
RT "Mammalian Sec61 is associated with Sec62 and Sec63.";
RL J. Biol. Chem. 275:14550-14557(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-556.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, and Leukocyte;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-760.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP TISSUE SPECIFICITY, AND VARIANT PCLD2 GLU-568 DEL.
RX PubMed=15133510; DOI=10.1038/ng1357;
RA Davila S., Furu L., Gharavi A.G., Tian X., Onoe T., Qian Q., Li A., Cai Y.,
RA Kamath P.S., King B.F., Azurmendi P.J., Tahvanainen P., Kaeaeriaeinen H.,
RA Hoeckerstedt K., Devuyst O., Pirson Y., Martin R.S., Lifton R.P.,
RA Tahvanainen E., Torres V.E., Somlo S.;
RT "Mutations in SEC63 cause autosomal dominant polycystic liver disease.";
RL Nat. Genet. 36:575-577(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742 AND SER-748, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION.
RX PubMed=22375059; DOI=10.1242/jcs.096727;
RA Lang S., Benedix J., Fedeles S.V., Schorr S., Schirra C., Schaeuble N.,
RA Jalal C., Greiner M., Hassdenteufel S., Tatzelt J., Kreutzer B.,
RA Edelmann L., Krause E., Rettig J., Somlo S., Zimmermann R., Dudek J.;
RT "Different effects of Sec61alpha, Sec62 and Sec63 depletion on transport of
RT polypeptides into the endoplasmic reticulum of mammalian cells.";
RL J. Cell Sci. 125:1958-1969(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF HIS-132 AND 735-GLY--ASP-760.
RX PubMed=29719251; DOI=10.1016/j.celrep.2018.03.122;
RA Hassdenteufel S., Johnson N., Paton A.W., Paton J.C., High S.,
RA Zimmermann R.;
RT "Chaperone-Mediated Sec61 Channel Gating during ER Import of Small
RT Precursor Proteins Overcomes Sec61 Inhibitor-Reinforced Energy Barrier.";
RL Cell Rep. 23:1373-1386(2018).
RN [13]
RP INVOLVEMENT IN PCLD2, AND VARIANTS PCLD2 7-GLN--ASP-760 DEL;
RP 58-TRP--ASP-760 DEL; 98-ARG--ASP-760 DEL; 233-TYR--ASP-760 DEL;
RP 239-ARG--ASP-760 DEL; 297-TYR--ASP-760 DEL; 417-GLU--ASP-760 DEL;
RP 550-LYS--ASP-760 DEL AND 601-GLN--ASP-760 DEL.
RX PubMed=28375157; DOI=10.1172/jci90129;
RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M.,
RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E.,
RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P.,
RA Torres V.E., Somlo S.;
RT "Isolated polycystic liver disease genes define effectors of polycystin-1
RT function.";
RL J. Clin. Invest. 127:1772-1785(2017).
CC -!- FUNCTION: Mediates cotranslational and post-translational transport of
CC certain precursor polypeptides across endoplasmic reticulum (ER)
CC (PubMed:22375059, PubMed:29719251). Proposed to play an auxiliary role
CC in recognition of precursors with short and apolar signal peptides. May
CC cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small
CC presecretory proteins into the SEC61 channel-forming translocon
CC complex, triggering channel opening for polypeptide translocation to
CC the ER lumen (PubMed:29719251). Required for efficient PKD1/Polycystin-
CC 1 biogenesis and trafficking to the plasma membrane of the primary
CC cilia (By similarity). {ECO:0000250|UniProtKB:Q8VHE0,
CC ECO:0000269|PubMed:22375059, ECO:0000269|PubMed:29719251}.
CC -!- SUBUNIT: The ER translocon complex consists of channel-forming core
CC components SEC61A1, SEC61B and SEC61G and different auxiliary
CC components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P82008}.
CC -!- INTERACTION:
CC Q9UGP8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1045560, EBI-16439278;
CC Q9UGP8; P97346: Nxn; Xeno; NbExp=6; IntAct=EBI-1045560, EBI-309684;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in the liver.
CC {ECO:0000269|PubMed:15133510}.
CC -!- DISEASE: Polycystic liver disease 2 with or without kidney cysts
CC (PCLD2) [MIM:617004]: An autosomal dominant hepatobiliary disease
CC characterized by overgrowth of biliary epithelium and supportive
CC connective tissue, resulting in multiple liver cysts. A subset of
CC patients may develop kidney cysts that usually do not result in
CC clinically significant renal disease. {ECO:0000269|PubMed:15133510,
CC ECO:0000269|PubMed:28375157}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23598.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ011779; CAB46275.1; -; mRNA.
DR EMBL; AF100141; AAC83375.1; -; mRNA.
DR EMBL; AL024507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023598; AAH23598.1; ALT_SEQ; mRNA.
DR EMBL; BC047221; AAH47221.1; -; mRNA.
DR EMBL; BC048287; AAH48287.1; -; mRNA.
DR EMBL; AL137338; CAB70701.1; -; mRNA.
DR CCDS; CCDS5061.1; -.
DR PIR; T46504; T46504.
DR RefSeq; NP_009145.1; NM_007214.4.
DR AlphaFoldDB; Q9UGP8; -.
DR BioGRID; 116397; 334.
DR IntAct; Q9UGP8; 38.
DR MINT; Q9UGP8; -.
DR STRING; 9606.ENSP00000357998; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR CarbonylDB; Q9UGP8; -.
DR GlyGen; Q9UGP8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UGP8; -.
DR PhosphoSitePlus; Q9UGP8; -.
DR SwissPalm; Q9UGP8; -.
DR BioMuta; SEC63; -.
DR DMDM; 18203500; -.
DR EPD; Q9UGP8; -.
DR jPOST; Q9UGP8; -.
DR MassIVE; Q9UGP8; -.
DR MaxQB; Q9UGP8; -.
DR PaxDb; Q9UGP8; -.
DR PeptideAtlas; Q9UGP8; -.
DR PRIDE; Q9UGP8; -.
DR ProteomicsDB; 84254; -.
DR Antibodypedia; 32190; 139 antibodies from 23 providers.
DR DNASU; 11231; -.
DR Ensembl; ENST00000369002.9; ENSP00000357998.4; ENSG00000025796.14.
DR GeneID; 11231; -.
DR KEGG; hsa:11231; -.
DR MANE-Select; ENST00000369002.9; ENSP00000357998.4; NM_007214.5; NP_009145.1.
DR UCSC; uc003psc.5; human.
DR CTD; 11231; -.
DR DisGeNET; 11231; -.
DR GeneCards; SEC63; -.
DR HGNC; HGNC:21082; SEC63.
DR HPA; ENSG00000025796; Low tissue specificity.
DR MalaCards; SEC63; -.
DR MIM; 608648; gene.
DR MIM; 617004; phenotype.
DR neXtProt; NX_Q9UGP8; -.
DR OpenTargets; ENSG00000025796; -.
DR Orphanet; 2924; Isolated polycystic liver disease.
DR PharmGKB; PA134936990; -.
DR VEuPathDB; HostDB:ENSG00000025796; -.
DR eggNOG; KOG0721; Eukaryota.
DR GeneTree; ENSGT00390000001965; -.
DR HOGENOM; CLU_014210_1_0_1; -.
DR InParanoid; Q9UGP8; -.
DR OMA; RAILHAH; -.
DR OrthoDB; 686427at2759; -.
DR PhylomeDB; Q9UGP8; -.
DR TreeFam; TF105904; -.
DR PathwayCommons; Q9UGP8; -.
DR SignaLink; Q9UGP8; -.
DR SIGNOR; Q9UGP8; -.
DR BioGRID-ORCS; 11231; 405 hits in 1078 CRISPR screens.
DR ChiTaRS; SEC63; human.
DR GeneWiki; SEC63; -.
DR GenomeRNAi; 11231; -.
DR Pharos; Q9UGP8; Tbio.
DR PRO; PR:Q9UGP8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UGP8; protein.
DR Bgee; ENSG00000025796; Expressed in colonic epithelium and 215 other tissues.
DR ExpressionAtlas; Q9UGP8; baseline and differential.
DR Genevisible; Q9UGP8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031207; C:Sec62/Sec63 complex; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:Ensembl.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:MGI.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; TAS:ProtInc.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:MGI.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027137; Sec63.
DR InterPro; IPR004179; Sec63-dom.
DR PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF02889; Sec63; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Disease variant; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..760
FT /note="Translocation protein SEC63 homolog"
FT /id="PRO_0000071097"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..188
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..165
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 197..541
FT /note="SEC63 1"
FT DOMAIN 637..714
FT /note="SEC63 2"
FT REGION 492..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..635
FT /evidence="ECO:0000255"
FT COMPBIAS 520..535
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..760
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 7..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080944"
FT VARIANT 58..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080945"
FT VARIANT 98..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080946"
FT VARIANT 233..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080947"
FT VARIANT 239..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080948"
FT VARIANT 297..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080949"
FT VARIANT 417..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080950"
FT VARIANT 550..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080951"
FT VARIANT 556
FT /note="V -> I (in dbSNP:rs17854547)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_061146"
FT VARIANT 568
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:15133510"
FT /id="VAR_019645"
FT VARIANT 601..760
FT /note="Missing (in PCLD2)"
FT /evidence="ECO:0000269|PubMed:28375157"
FT /id="VAR_080952"
FT MUTAGEN 132
FT /note="H->Q: Reduces cotranslational translocation of APLN
FT precursor/preproapelin."
FT /evidence="ECO:0000269|PubMed:29719251"
FT MUTAGEN 735..760
FT /note="Missing: Reduces cotranslational translocation of
FT APLN precursor/preproapelin."
FT /evidence="ECO:0000269|PubMed:29719251"
FT CONFLICT 115
FT /note="A -> V (in Ref. 4; AAH23598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 87997 MW; 81BBF269A3FCCF0D CRC64;
MAGQQFQYDD SGNTFFYFLT SFVGLIVIPA TYYLWPRDQN AEQIRLKNIR KVYGRCMWYR
LRLLKPQPNI IPTVKKIVLL AGWALFLFLA YKVSKTDREY QEYNPYEVLN LDPGATVAEI
KKQYRLLSLK YHPDKGGDEV MFMRIAKAYA ALTDEESRKN WEEFGNPDGP QATSFGIALP
AWIVDQKNSI LVLLVYGLAF MVILPVVVGS WWYRSIRYSG DQILIRTTQI YTYFVYKTRN
MDMKRLIMVL AGASEFDPQY NKDATSRPTD NILIPQLIRE IGSINLKKNE PPLTCPYSLK
ARVLLLSHLA RMKIPETLEE DQQFMLKKCP ALLQEMVNVI CQLIVMARNR EEREFRAPTL
ASLENCMKLS QMAVQGLQQF KSPLLQLPHI EEDNLRRVSN HKKYKIKTIQ DLVSLKESDR
HTLLHFLEDE KYEEVMAVLG SFPYVTMDIK SQVLDDEDSN NITVGSLVTV LVKLTRQTMA
EVFEKEQSIC AAEEQPAEDG QGETNKNRTK GGWQQKSKGP KKTAKSKKKK PLKKKPTPVL
LPQSKQQKQK QANGVVGNEA AVKEDEEEVS DKGSDSEEEE TNRDSQSEKD DGSDRDSDRE
QDEKQNKDDE AEWQELQQSI QRKERALLET KSKITHPVYS LYFPEEKQEW WWLYIADRKE
QTLISMPYHV CTLKDTEEVE LKFPAPGKPG NYQYTVFLRS DSYMGLDQIK PLKLEVHEAK
PVPENHPQWD TAIEGDEDQE DSEGFEDSFE EEEEEEEDDD
