S61A1_HUMAN
ID S61A1_HUMAN Reviewed; 476 AA.
AC P61619; P38378; P57726; Q5JPF8; Q8N0Z4; Q8N3U3; Q8NC71; Q9BU16; Q9Y2R3;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein transport protein Sec61 subunit alpha isoform 1;
DE Short=Sec61 alpha-1;
GN Name=SEC61A1; Synonyms=SEC61A;
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].
RA Liu T., Zhang J., Ye M., Zhang Q., Fu G., Zhou J., Wu J., Shen Y., Yu M.,
RA Chen S., Mao M., Chen Z.;
RT "Human sec61 homolog gene.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li W., Liu T., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y., Yu M.,
RA Chen S., Mao M., Chen Z.;
RT "Human sec61 homolog gene mRNA sequence.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Finke K., Prehn S., Hartmann E.;
RT "Sec61 alpha isoforms.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, and Lymph node;
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 FUNCTION.
RX PubMed=8616892; DOI=10.1016/s0092-8674(00)81115-0;
RA Do H., Falcone D., Lin J., Andrews D.W., Johnson A.E.;
RT "The cotranslational integration of membrane proteins into the phospholipid
RT bilayer is a multistep process.";
RL Cell 85:369-378(1996).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12475939; DOI=10.1091/mbc.e02-04-0198;
RA Meacock S.L., Lecomte F.J., Crawshaw S.G., High S.;
RT "Different transmembrane domains associate with distinct endoplasmic
RT reticulum components during membrane integration of a polytopic protein.";
RL Mol. Biol. Cell 13:4114-4129(2002).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 TYR-344.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32814900; DOI=10.1038/s41586-020-2624-y;
RA Chitwood P.J., Hegde R.S.;
RT "An intramembrane chaperone complex facilitates membrane protein
RT biogenesis.";
RL Nature 584:630-634(2020).
RN [14]
RP FUNCTION, AND INTERACTION WITH TMCO1; CCDC47; NCLN; NOMO; TMEM147; SEC61A1
RP AND SEC61B.
RX PubMed=32820719; DOI=10.7554/elife.56889;
RA McGilvray P.T., Anghel S.A., Sundaram A., Zhong F., Trnka M.J.,
RA Fuller J.R., Hu H., Burlingame A.L., Keenan R.J.;
RT "An ER translocon for multi-pass membrane protein biogenesis.";
RL Elife 9:0-0(2020).
RN [15]
RP VARIANTS ADTKD5 GLY-67 AND ALA-185, CHARACTERIZATION OF VARIANTS ADTKD5
RP GLY-67 AND ALA-185, INVOLVEMENT IN ADTKD5, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=27392076; DOI=10.1016/j.ajhg.2016.05.028;
RA Bolar N.A., Golzio C., Zivna M., Hayot G., Van Hemelrijk C., Schepers D.,
RA Vandeweyer G., Hoischen A., Huyghe J.R., Raes A., Matthys E., Sys E.,
RA Azou M., Gubler M.C., Praet M., Van Camp G., McFadden K., Pediaditakis I.,
RA Pristoupilova A., Hodanova K., Vyletal P., Hartmannova H., Stranecky V.,
RA Hulkova H., Baresova V., Jedlickova I., Sovova J., Hnizda A., Kidd K.,
RA Bleyer A.J., Spong R.S., Vande Walle J., Mortier G., Brunner H.,
RA Van Laer L., Kmoch S., Katsanis N., Loeys B.L.;
RT "Heterozygous loss-of-function SEC61A1 mutations cause autosomal-dominant
RT tubulo-interstitial and glomerulocystic kidney disease with anemia.";
RL Am. J. Hum. Genet. 99:174-187(2016).
RN [16]
RP FUNCTION, VARIANT ASP-85, AND CHARACTERIZATION OF VARIANT ASP-85.
RX PubMed=28782633; DOI=10.1016/j.jaci.2017.06.042;
RA Schubert D., Klein M.C., Hassdenteufel S., Caballero-Oteyza A., Yang L.,
RA Proietti M., Bulashevska A., Kemming J., Kuehn J., Winzer S., Rusch S.,
RA Fliegauf M., Schaeffer A.A., Pfeffer S., Geiger R., Cavalie A., Cao H.,
RA Yang F., Li Y., Rizzi M., Eibel H., Kobbe R., Marks A.L., Peppers B.P.,
RA Hostoffer R.W., Puck J.M., Zimmermann R., Grimbacher B.;
RT "Plasma cell deficiency in human subjects with heterozygous mutations in
RT Sec61 translocon alpha 1 subunit (SEC61A1).";
RL J. Allergy Clin. Immunol. 141:1427-1438(2018).
CC -!- FUNCTION: Component of SEC61 channel-forming translocon complex that
CC mediates transport of signal peptide-containing precursor polypeptides
CC across the endoplasmic reticulum (ER) (PubMed:12475939,
CC PubMed:22375059, PubMed:29719251, PubMed:32814900, PubMed:28782633).
CC Forms a ribosome receptor and a gated pore in the ER membrane, both
CC functions required for cotranslational translocation of nascent
CC polypeptides (PubMed:22375059, PubMed:29719251, PubMed:28782633). May
CC cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable
CC post-translational transport of small presecretory proteins
CC (PubMed:22375059, PubMed:29719251). Component of a ribosome-associated
CC ER translocon complex involved in multi-pass membrane protein transport
CC into the ER membrane and biogenesis (PubMed:32820719). The SEC61
CC channel cooperates with the translocating protein TRAM1 to import
CC nascent proteins into the ER (PubMed:8616892). Controls the passive
CC efflux of calcium ions from the ER lumen to the cytosol through SEC61
CC channel, contributing to the maintenance of cellular calcium
CC homeostasis (PubMed:28782633). Plays a critical role in nephrogenesis,
CC specifically at pronephros stage (By similarity).
CC {ECO:0000250|UniProtKB:P61620, ECO:0000269|PubMed:12475939,
CC ECO:0000269|PubMed:22375059, ECO:0000269|PubMed:28782633,
CC ECO:0000269|PubMed:29719251, ECO:0000269|PubMed:32814900,
CC ECO:0000269|PubMed:32820719, ECO:0000269|PubMed:8616892}.
CC -!- SUBUNIT: The SEC61 channel-forming translocon complex consists of
CC channel-forming core components SEC61A1, SEC61B and SEC61G and
CC different auxiliary components such as SEC62 and SEC63 (By similarity).
CC The ribosome-associated ER translocon complex includes SEC61A1, SEC61B,
CC SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence
CC of ribosomes, only the complex forms with NCLN/Nicalin, NOMO and
CC TMEM147 remains intact (PubMed:32820719).
CC {ECO:0000250|UniProtKB:P38377, ECO:0000269|PubMed:32820719}.
CC -!- INTERACTION:
CC P61619; P27824: CANX; NbExp=4; IntAct=EBI-358919, EBI-355947;
CC P61619; P11021: HSPA5; NbExp=3; IntAct=EBI-358919, EBI-354921;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:27392076,
CC ECO:0000269|PubMed:32814900, ECO:0000269|PubMed:8616892}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Localizes exclusively in granular
CC structures in the endoplasmic reticulum (ER).
CC {ECO:0000269|PubMed:27392076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61619-1; Sequence=Displayed;
CC Name=3;
CC IsoId=P61619-3; Sequence=VSP_013747;
CC -!- TISSUE SPECIFICITY: Expressed in proximal and distal tubules in kidney
CC (at protein level). {ECO:0000269|PubMed:28782633}.
CC -!- DISEASE: Tubulointerstitial kidney disease, autosomal dominant, 5
CC (ADTKD5) [MIM:617056]: A form of autosomal dominant tubulointerstitial
CC kidney disease, a genetically heterogeneous disorder characterized by
CC slowly progressive loss of kidney function, bland urinary sediment,
CC hyperuricemia, absent or mildly increased albuminuria, lack of severe
CC hypertension during the early stages, and normal or small kidneys on
CC ultrasound. Renal histology shows variable abnormalities including
CC interstitial fibrosis with tubular atrophy, microcystic dilatation of
CC the tubules, thickening of tubular basement membranes, medullary cysts,
CC and secondary glomerulosclerotic or glomerulocystic changes with
CC abnormal glomerular tufting. There is significant variability, as well
CC as incomplete penetrance. {ECO:0000269|PubMed:27392076}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Defects in SEC61A1 may be a cause of autosomal dominant
CC hypogammaglobulinemia, resulting in severe recurrent infections, mainly
CC of the respiratory tract. Disease onset is mostly in the first year of
CC life. Affected subjects manifest reduced antibodies production by
CC plasma cells, in the presence of normal subpopulations of B and T cells
CC in the peripheral blood. Patients respond well to immunoglobulin
CC replacement therapy. {ECO:0000269|PubMed:28782633}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11283.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11434.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF077032; AAD27765.1; -; mRNA.
DR EMBL; AF084458; AAD39847.1; -; mRNA.
DR EMBL; AF346602; AAK29083.1; -; mRNA.
DR EMBL; AK074907; BAC11283.1; ALT_INIT; mRNA.
DR EMBL; AK074928; BAC11298.1; -; mRNA.
DR EMBL; AK075148; BAC11434.1; ALT_INIT; mRNA.
DR EMBL; AL831940; CAD38592.1; -; mRNA.
DR EMBL; AL832821; CAI46127.1; -; mRNA.
DR CCDS; CCDS3046.1; -. [P61619-1]
DR RefSeq; NP_037468.1; NM_013336.3. [P61619-1]
DR PDB; 6W6L; EM; 3.84 A; 1=1-476.
DR PDBsum; 6W6L; -.
DR AlphaFoldDB; P61619; -.
DR SMR; P61619; -.
DR BioGRID; 118968; 160.
DR IntAct; P61619; 60.
DR MINT; P61619; -.
DR STRING; 9606.ENSP00000243253; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; P61619; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61619; -.
DR MetOSite; P61619; -.
DR PhosphoSitePlus; P61619; -.
DR SwissPalm; P61619; -.
DR BioMuta; SEC61A1; -.
DR DMDM; 48429109; -.
DR EPD; P61619; -.
DR jPOST; P61619; -.
DR MassIVE; P61619; -.
DR MaxQB; P61619; -.
DR PaxDb; P61619; -.
DR PeptideAtlas; P61619; -.
DR PRIDE; P61619; -.
DR ProteomicsDB; 57326; -. [P61619-1]
DR ProteomicsDB; 57327; -. [P61619-3]
DR Antibodypedia; 17274; 185 antibodies from 34 providers.
DR DNASU; 29927; -.
DR Ensembl; ENST00000243253.8; ENSP00000243253.3; ENSG00000058262.10. [P61619-1]
DR Ensembl; ENST00000424880.2; ENSP00000411445.2; ENSG00000058262.10. [P61619-3]
DR GeneID; 29927; -.
DR KEGG; hsa:29927; -.
DR MANE-Select; ENST00000243253.8; ENSP00000243253.3; NM_013336.4; NP_037468.1.
DR UCSC; uc003ekb.4; human. [P61619-1]
DR CTD; 29927; -.
DR DisGeNET; 29927; -.
DR GeneCards; SEC61A1; -.
DR HGNC; HGNC:18276; SEC61A1.
DR HPA; ENSG00000058262; Low tissue specificity.
DR MalaCards; SEC61A1; -.
DR MIM; 609213; gene.
DR MIM; 617056; phenotype.
DR neXtProt; NX_P61619; -.
DR OpenTargets; ENSG00000058262; -.
DR PharmGKB; PA134901772; -.
DR VEuPathDB; HostDB:ENSG00000058262; -.
DR eggNOG; KOG1373; Eukaryota.
DR GeneTree; ENSGT00390000003721; -.
DR HOGENOM; CLU_031763_2_0_1; -.
DR InParanoid; P61619; -.
DR OMA; VIEDPMH; -.
DR PhylomeDB; P61619; -.
DR TreeFam; TF300348; -.
DR PathwayCommons; P61619; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; P61619; -.
DR SIGNOR; P61619; -.
DR BioGRID-ORCS; 29927; 750 hits in 1086 CRISPR screens.
DR ChiTaRS; SEC61A1; human.
DR GeneWiki; Sec61_alpha_1; -.
DR GenomeRNAi; 29927; -.
DR Pharos; P61619; Tbio.
DR PRO; PR:P61619; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P61619; protein.
DR Bgee; ENSG00000058262; Expressed in body of pancreas and 196 other tissues.
DR ExpressionAtlas; P61619; baseline and differential.
DR Genevisible; P61619; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
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:0039019; P:pronephric nephron development; ISS:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:UniProtKB.
DR GO; GO:0045047; P:protein targeting to ER; ISS:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:MGI.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.3370.10; -; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Disease variant;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..476
FT /note="Protein transport protein Sec61 subunit alpha
FT isoform 1"
FT /id="PRO_0000131791"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..76
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..144
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..240
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..445
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013747"
FT VARIANT 67
FT /note="V -> G (in ADTKD5; decreases in protein stability;
FT partly confers novel Golgi subcellular location;
FT dbSNP:rs752745051)"
FT /evidence="ECO:0000269|PubMed:27392076"
FT /id="VAR_077059"
FT VARIANT 85
FT /note="V -> D (probable disease-associated variant found in
FT a family with hypogammaglobulinemia; decreased function in
FT cotranslational protein targeting to endoplasmic reticulum;
FT dbSNP:rs1553721236)"
FT /evidence="ECO:0000269|PubMed:28782633"
FT /id="VAR_080231"
FT VARIANT 185
FT /note="T -> A (in ADTKD5; decreases in protein stability;
FT partly confers novel Golgi subcellular location;
FT dbSNP:rs879255648)"
FT /evidence="ECO:0000269|PubMed:27392076"
FT /id="VAR_077060"
FT MUTAGEN 344
FT /note="Y->H: Reduces cotranslational translocation of APLN
FT precursor/preproapelin."
FT /evidence="ECO:0000269|PubMed:29719251"
FT CONFLICT 135
FT /note="G -> W (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="F -> L (in Ref. 4; BAC11298)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="T -> S (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="A -> V (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> F (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> N (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 323..329
FT /note="TWSDTSS -> QWADVSG (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="A -> S (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..355
FT /note="FGSVL -> MGAIF (in Ref. 1; AAD27765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52265 MW; 44A9B7B37C7C82E4 CRC64;
MAIKFLEVIK PFCVILPEIQ KPERKIQFKE KVLWTAITLF IFLVCCQIPL FGIMSSDSAD
PFYWMRVILA SNRGTLMELG ISPIVTSGLI MQLLAGAKII EVGDTPKDRA LFNGAQKLFG
MIITIGQSIV YVMTGMYGDP SEMGAGICLL ITIQLFVAGL IVLLLDELLQ KGYGLGSGIS
LFIATNICET IVWKAFSPTT VNTGRGMEFE GAIIALFHLL ATRTDKVRAL REAFYRQNLP
NLMNLIATIF VFAVVIYFQG FRVDLPIKSA RYRGQYNTYP IKLFYTSNIP IILQSALVSN
LYVISQMLSA RFSGNLLVSL LGTWSDTSSG GPARAYPVGG LCYYLSPPES FGSVLEDPVH
AVVYIVFMLG SCAFFSKTWI EVSGSSAKDV AKQLKEQQMV MRGHRETSMV HELNRYIPTA
AAFGGLCIGA LSVLADFLGA IGSGTGILLA VTIIYQYFEI FVKEQSEVGS MGALLF
