ID   AMNLS_HUMAN             Reviewed;         453 AA.
AC   Q9BXJ7; Q6UX83;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Protein amnionless;
DE   Contains:
DE     RecName: Full=Soluble protein amnionless;
DE   Flags: Precursor;
GN   Name=AMN; ORFNames=UNQ513/PRO1028;
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=11279523; DOI=10.1038/86912;
RA   Kalantry S., Manning S., Haub O., Tomihara-Newberger C., Lee H.-G.,
RA   Fangman J., Disteche C.M., Manova K., Lacy E.;
RT   "The amnionless gene, essential for mouse gastrulation, encodes a visceral-
RT   endoderm-specific protein with an extracellular cysteine-rich domain.";
RL   Nat. Genet. 27:412-416(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-230.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 300-323 AND 393-453, TISSUE SPECIFICITY, VARIANT IGS2
RP   ILE-41, FUNCTION, AND ALTERNATIVE PRODUCTS.
RX   PubMed=12590260; DOI=10.1038/ng1098;
RA   Tanner S.M., Aminoff M., Wright F.A., Liyanarachchi S., Kuronen M.,
RA   Saarinen A., Massika O., Mandel H., Broch H., de la Chapelle A.;
RT   "Amnionless, essential for mouse gastrulation, is mutated in recessive
RT   hereditary megaloblastic anemia.";
RL   Nat. Genet. 33:426-429(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH CUBN,
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX   PubMed=14576052; DOI=10.1182/blood-2003-08-2852;
RA   Fyfe J.C., Madsen M., Hoejrup P., Christensen E.I., Tanner S.M.,
RA   de la Chapelle A., He Q., Moestrup S.K.;
RT   "The functional cobalamin (vitamin B12)-intrinsic factor receptor is a
RT   novel complex of cubilin and amnionless.";
RL   Blood 103:1573-1579(2004).
RN   [6] {ECO:0007744|PDB:6GJE}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-357 IN COMPLEX WITH CUBN,
RP   CHARACTERIZATION OF VARIANT IGS2 ILE-41, SUBUNIT, SUBCELLULAR LOCATION,
RP   TOPOLOGY, DISULFIDE BONDS, AND MUTAGENESIS OF ASN-35 AND SER-37.
RX   PubMed=30523278; DOI=10.1038/s41467-018-07468-4;
RA   Larsen C., Etzerodt A., Madsen M., Skjodt K., Moestrup S.K.,
RA   Andersen C.B.F.;
RT   "Structural assembly of the megadalton-sized receptor for intestinal
RT   vitamin B12 uptake and kidney protein reabsorption.";
RL   Nat. Commun. 9:5204-5204(2018).
RN   [7]
RP   VARIANTS IGS2 ILE-41 AND PHE-234.
RX   PubMed=22929189; DOI=10.1186/1750-1172-7-56;
RA   Tanner S.M., Sturm A.C., Baack E.C., Liyanarachchi S., de la Chapelle A.;
RT   "Inherited cobalamin malabsorption. Mutations in three genes reveal
RT   functional and ethnic patterns.";
RL   Orphanet J. Rare Dis. 7:56-56(2012).
RN   [8]
RP   VARIANT IGS2 LYS-69, AND FUNCTION.
RX   PubMed=26040326; DOI=10.1186/s12881-015-0181-2;
RA   Montgomery E., Sayer J.A., Baines L.A., Hynes A.M., Vega-Warner V.,
RA   Johnson S., Goodship J.A., Otto E.A.;
RT   "Novel compound heterozygous mutations in AMN cause Imerslund-Graesbeck
RT   syndrome in two half-sisters: a case report.";
RL   BMC Med. Genet. 16:35-35(2015).
RN   [9]
RP   INVOLVEMENT IN IGS2.
RX   PubMed=22631584; DOI=10.1111/j.1442-200x.2011.03482.x;
RA   Densupsoontorn N., Sanpakit K., Vijarnsorn C., Pattaragarn A.,
RA   Kangwanpornsiri C., Jatutipsompol C., Tirapongporn H., Jirapinyo P.,
RA   Shah N.P., Sturm A.C., Tanner S.M.;
RT   "Imerslund-Grasbeck syndrome: new mutation in amnionless.";
RL   Pediatr. Int. 54:E19-E21(2012).
RN   [10]
RP   FUNCTION, INTERACTION WITH CUBN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   CHARACTERIZATION OF VARIANTS IGS2 ILE-41; LYS-69 AND PHE-234, AND
RP   MUTAGENESIS OF LEU-59 AND GLY-254.
RX   PubMed=29402915; DOI=10.1038/s41598-018-20731-4;
RA   Udagawa T., Harita Y., Miura K., Mitsui J., Ode K.L., Morishita S.,
RA   Urae S., Kanda S., Kajiho Y., Tsurumi H., Ueda H.R., Tsuji S., Saito A.,
RA   Oka A.;
RT   "Amnionless-mediated glycosylation is crucial for cell surface targeting of
RT   cubilin in renal and intestinal cells.";
RL   Sci. Rep. 8:2351-2351(2018).
CC   -!- FUNCTION: Membrane-bound component of the endocytic receptor formed by
CC       AMN and CUBN (PubMed:14576052, PubMed:30523278, PubMed:29402915).
CC       Required for normal CUBN glycosylation and trafficking to the cell
CC       surface (PubMed:14576052, PubMed:29402915). The complex formed by AMN
CC       and CUBN is required for efficient absorption of vitamin B12
CC       (PubMed:12590260, PubMed:14576052, PubMed:26040326). Required for
CC       normal CUBN-mediated protein transport in the kidney (Probable).
CC       {ECO:0000269|PubMed:12590260, ECO:0000269|PubMed:14576052,
CC       ECO:0000269|PubMed:26040326, ECO:0000269|PubMed:29402915,
CC       ECO:0000269|PubMed:30523278, ECO:0000305|PubMed:22631584,
CC       ECO:0000305|PubMed:26040326}.
CC   -!- SUBUNIT: Interacts (via extracellular region) with CUBN/cubilin, giving
CC       rise to a huge complex containing one AMN chain and three CUBN chains.
CC       {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915,
CC       ECO:0000269|PubMed:30523278}.
CC   -!- INTERACTION:
CC       Q9BXJ7; O60494: CUBN; NbExp=3; IntAct=EBI-11510881, EBI-3953632;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane
CC       {ECO:0000269|PubMed:14576052}; Single-pass type I membrane protein
CC       {ECO:0000305|PubMed:30523278}. Cell membrane
CC       {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915,
CC       ECO:0000269|PubMed:30523278}; Single-pass type I membrane protein
CC       {ECO:0000305}. Endosome membrane {ECO:0000305|PubMed:14576052}.
CC       Membrane, coated pit {ECO:0000305|PubMed:14576052}.
CC   -!- SUBCELLULAR LOCATION: [Soluble protein amnionless]: Secreted
CC       {ECO:0000269|PubMed:14576052}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=1;
CC         Comment=At least 5 isoforms, 1, 2, 3, 4 and 5, are produced.
CC         {ECO:0000305|PubMed:12590260};
CC       Name=1;
CC         IsoId=Q9BXJ7-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Detected in proximal tubules in the kidney cortex
CC       (at protein level) (PubMed:14576052, PubMed:29402915). Long isoforms
CC       are highly expressed in small intestine, colon and kidney (renal
CC       proximal tubule epithelial cells). Shorter isoforms are detected at
CC       lower levels in testis, thymus and peripheral blood leukocytes.
CC       {ECO:0000269|PubMed:12590260, ECO:0000269|PubMed:14576052,
CC       ECO:0000269|PubMed:29402915}.
CC   -!- DOMAIN: The complex formed by AMN and CUBN is composed of a 400
CC       Angstrom long stem and a globular crown region. The stem region is
CC       probably formed by AMN and the CUBN N-terminal region, including the
CC       EGF-like domains. The crown is probably formed by the CUBN CUB domains.
CC       {ECO:0000250|UniProtKB:F1SAM7}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14576052}.
CC   -!- PTM: A soluble form arises by proteolytic removal of the membrane
CC       anchor. {ECO:0000269|PubMed:14576052}.
CC   -!- DISEASE: Imerslund-Grasbeck syndrome 2 (IGS2) [MIM:618882]: A form of
CC       Imerslund-Grasbeck syndrome, a rare autosomal recessive disorder
CC       characterized by vitamin B12 deficiency commonly resulting in
CC       megaloblastic anemia, which is responsive to parenteral vitamin B12
CC       therapy and appears in infancy or early childhood. Clinical
CC       manifestations include failure to thrive, infections and neurological
CC       damage. Mild proteinuria, with no signs of kidney disease, is present
CC       in about half of the patients. {ECO:0000269|PubMed:12590260,
CC       ECO:0000269|PubMed:22631584, ECO:0000269|PubMed:22929189,
CC       ECO:0000269|PubMed:26040326, ECO:0000269|PubMed:29402915,
CC       ECO:0000269|PubMed:30523278}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: The role of Amn in embryonic development seems to be
CC       species specific. In mice, null mutations lead to embryonic lethality.
CC       Human mutations give rise to much milder symptoms. {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; AF328788; AAK28532.1; -; mRNA.
DR   EMBL; AL117209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY358468; AAQ89949.1; -; mRNA.
DR   CCDS; CCDS9977.1; -. [Q9BXJ7-1]
DR   RefSeq; NP_112205.2; NM_030943.3. [Q9BXJ7-1]
DR   PDB; 6GJE; X-ray; 2.30 A; A=20-359.
DR   PDBsum; 6GJE; -.
DR   AlphaFoldDB; Q9BXJ7; -.
DR   SMR; Q9BXJ7; -.
DR   BioGRID; 123571; 1.
DR   ComplexPortal; CPX-5774; Cubam cobalamin uptake receptor complex.
DR   CORUM; Q9BXJ7; -.
DR   IntAct; Q9BXJ7; 2.
DR   STRING; 9606.ENSP00000299155; -.
DR   DrugBank; DB00115; Cyanocobalamin.
DR   DrugBank; DB00200; Hydroxocobalamin.
DR   DrugCentral; Q9BXJ7; -.
DR   GlyCosmos; Q9BXJ7; 1 site, No reported glycans.
DR   GlyGen; Q9BXJ7; 1 site.
DR   iPTMnet; Q9BXJ7; -.
DR   PhosphoSitePlus; Q9BXJ7; -.
DR   BioMuta; AMN; -.
DR   DMDM; 296434395; -.
DR   jPOST; Q9BXJ7; -.
DR   MassIVE; Q9BXJ7; -.
DR   MaxQB; Q9BXJ7; -.
DR   PaxDb; 9606-ENSP00000299155; -.
DR   PeptideAtlas; Q9BXJ7; -.
DR   ProteomicsDB; 79440; -. [Q9BXJ7-1]
DR   Antibodypedia; 13; 57 antibodies from 22 providers.
DR   DNASU; 81693; -.
DR   Ensembl; ENST00000299155.10; ENSP00000299155.6; ENSG00000166126.11. [Q9BXJ7-1]
DR   GeneID; 81693; -.
DR   KEGG; hsa:81693; -.
DR   MANE-Select; ENST00000299155.10; ENSP00000299155.6; NM_030943.4; NP_112205.2.
DR   UCSC; uc001ymg.5; human. [Q9BXJ7-1]
DR   AGR; HGNC:14604; -.
DR   CTD; 81693; -.
DR   DisGeNET; 81693; -.
DR   GeneCards; AMN; -.
DR   HGNC; HGNC:14604; AMN.
DR   HPA; ENSG00000166126; Group enriched (intestine, kidney, liver).
DR   MalaCards; AMN; -.
DR   MIM; 605799; gene.
DR   MIM; 618882; phenotype.
DR   neXtProt; NX_Q9BXJ7; -.
DR   OpenTargets; ENSG00000166126; -.
DR   Orphanet; 35858; Imerslund-Graesbeck syndrome.
DR   PharmGKB; PA134962814; -.
DR   VEuPathDB; HostDB:ENSG00000166126; -.
DR   eggNOG; ENOG502QUUQ; Eukaryota.
DR   GeneTree; ENSGT00390000007463; -.
DR   HOGENOM; CLU_050471_0_0_1; -.
DR   InParanoid; Q9BXJ7; -.
DR   OMA; PDRFSWL; -.
DR   OrthoDB; 2881963at2759; -.
DR   PhylomeDB; Q9BXJ7; -.
DR   TreeFam; TF323790; -.
DR   PathwayCommons; Q9BXJ7; -.
DR   Reactome; R-HSA-3359462; Defective AMN causes MGA1.
DR   Reactome; R-HSA-3359463; Defective CUBN causes MGA1.
DR   Reactome; R-HSA-8964011; HDL clearance.
DR   Reactome; R-HSA-9758881; Uptake of dietary cobalamins into enterocytes.
DR   SignaLink; Q9BXJ7; -.
DR   BioGRID-ORCS; 81693; 15 hits in 1146 CRISPR screens.
DR   GeneWiki; Amnionless; -.
DR   GenomeRNAi; 81693; -.
DR   Pharos; Q9BXJ7; Tbio.
DR   PRO; PR:Q9BXJ7; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9BXJ7; Protein.
DR   Bgee; ENSG00000166126; Expressed in mucosa of transverse colon and 169 other cell types or tissues.
DR   ExpressionAtlas; Q9BXJ7; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0031528; C:microvillus membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR   GO; GO:0038024; F:cargo receptor activity; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR   GO; GO:0009235; P:cobalamin metabolic process; IDA:MGI.
DR   GO; GO:0015889; P:cobalamin transport; IDA:UniProtKB.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR   GO; GO:0097017; P:renal protein absorption; IEA:Ensembl.
DR   InterPro; IPR026112; AMN.
DR   PANTHER; PTHR14995; AMNIONLESS; 1.
DR   PANTHER; PTHR14995:SF2; PROTEIN AMNIONLESS; 1.
DR   Pfam; PF14828; Amnionless; 1.
DR   Genevisible; Q9BXJ7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative promoter usage; Cell membrane; Coated pit;
KW   Developmental protein; Direct protein sequencing; Disease variant;
KW   Disulfide bond; Endosome; Glycoprotein; Membrane; Protein transport;
KW   Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:14576052"
FT   CHAIN           20..453
FT                   /note="Protein amnionless"
FT                   /id="PRO_0000020702"
FT   CHAIN           20..?
FT                   /note="Soluble protein amnionless"
FT                   /id="PRO_0000447651"
FT   TOPO_DOM        20..357
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:30523278"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        379..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          202..254
FT                   /note="VWFC"
FT   REGION          67..87
FT                   /note="Interaction with CUBN"
FT                   /evidence="ECO:0000269|PubMed:30523278"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..96
FT                   /evidence="ECO:0000269|PubMed:30523278,
FT                   ECO:0007744|PDB:6GJE"
FT   DISULFID        137..213
FT                   /evidence="ECO:0000269|PubMed:30523278,
FT                   ECO:0007744|PDB:6GJE"
FT   DISULFID        205..211
FT                   /evidence="ECO:0000269|PubMed:30523278,
FT                   ECO:0007744|PDB:6GJE"
FT   DISULFID        223..249
FT                   /evidence="ECO:0000269|PubMed:30523278,
FT                   ECO:0007744|PDB:6GJE"
FT   DISULFID        234..250
FT                   /evidence="ECO:0000269|PubMed:30523278,
FT                   ECO:0007744|PDB:6GJE"
FT   DISULFID        239..253
FT                   /evidence="ECO:0000269|PubMed:30523278,
FT                   ECO:0007744|PDB:6GJE"
FT   VARIANT         41
FT                   /note="T -> I (in IGS2; reduced presence at the cell
FT                   membrane; loss of interaction with CUBN; reduced CUBN
FT                   expression at the cell surface; dbSNP:rs119478058)"
FT                   /evidence="ECO:0000269|PubMed:12590260,
FT                   ECO:0000269|PubMed:22929189, ECO:0000269|PubMed:29402915,
FT                   ECO:0000269|PubMed:30523278"
FT                   /id="VAR_015733"
FT   VARIANT         69
FT                   /note="M -> K (in IGS2; loss of interaction with CUBN;
FT                   strongly reduced CUBN expression at the cell surface;
FT                   dbSNP:rs375774640)"
FT                   /evidence="ECO:0000269|PubMed:26040326"
FT                   /id="VAR_081906"
FT   VARIANT         234
FT                   /note="C -> F (in IGS2; loss of interaction with CUBN;
FT                   strongly reduced CUBN expression at the cell surface;
FT                   dbSNP:rs386834176)"
FT                   /evidence="ECO:0000269|PubMed:22929189,
FT                   ECO:0000269|PubMed:29402915"
FT                   /id="VAR_081907"
FT   MUTAGEN         35
FT                   /note="N->Q: Loss of expression at the cell membrane."
FT                   /evidence="ECO:0000269|PubMed:30523278"
FT   MUTAGEN         37
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:30523278"
FT   MUTAGEN         59
FT                   /note="L->P: Loss of interaction with CUBN and strongly
FT                   reduced CUBN expression at the cell surface."
FT                   /evidence="ECO:0000269|PubMed:29402915"
FT   MUTAGEN         254
FT                   /note="G->E: Loss of interaction with CUBN and strongly
FT                   reduced CUBN expression at the cell surface."
FT                   /evidence="ECO:0000269|PubMed:29402915"
FT   CONFLICT        241
FT                   /note="S -> F (in Ref. 1; AAK28532)"
FT                   /evidence="ECO:0000305"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          62..70
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   TURN            91..98
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           176..184
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           186..189
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          252..261
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           267..276
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   TURN            277..280
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           282..284
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          287..296
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          305..313
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   HELIX           320..339
FT                   /evidence="ECO:0007829|PDB:6GJE"
FT   STRAND          341..348
FT                   /evidence="ECO:0007829|PDB:6GJE"
SQ   SEQUENCE   453 AA;  47754 MW;  40AA14EF186A6009 CRC64;
     MGVLGRVLLW LQLCALTQAV SKLWVPNTDF DVAANWSQNR TPCAGGAVEF PADKMVSVLV
     QEGHAVSDML LPLDGELVLA SGAGFGVSDV GSHLDCGAGE PAVFRDSDRF SWHDPHLWRS
     GDEAPGLFFV DAERVPCRHD DVFFPPSASF RVGLGPGASP VRVRSISALG RTFTRDEDLA
     VFLASRAGRL RFHGPGALSV GPEDCADPSG CVCGNAEAQP WICAALLQPL GGRCPQAACH
     SALRPQGQCC DLCGAVVLLT HGPAFDLERY RARILDTFLG LPQYHGLQVA VSKVPRSSRL
     READTEIQVV LVENGPETGG AGRLARALLA DVAENGEALG VLEATMRESG AHVWGSSAAG
     LAGGVAAAVL LALLVLLVAP PLLRRAGRLR WRRHEAAAPA GAPLGFRNPV FDVTASEELP
     LPRRLSLVPK AAADSTSHSY FVNPLFAGAE AEA
//