ID EPB42_HUMAN Reviewed; 691 AA.
AC P16452; Q4KKX0; Q4VB97;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 24-JAN-2024, entry version 217.
DE RecName: Full=Protein 4.2 {ECO:0000305};
DE Short=P4.2 {ECO:0000305};
DE AltName: Full=Erythrocyte membrane protein band 4.2 {ECO:0000312|HGNC:HGNC:3381};
DE Short=Erythrocyte protein 4.2 {ECO:0000303|PubMed:1544941};
GN Name=EPB42 {ECO:0000312|HGNC:HGNC:3381}; Synonyms=E42P;
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] (ISOFORM LONG).
RC TISSUE=Reticulocyte;
RX PubMed=2052563; DOI=10.1073/pnas.88.11.4840;
RA Korsgren C., Cohen C.M.;
RT "Organization of the gene for human erythrocyte membrane protein 4.2:
RT structural similarities with the gene for the a subunit of factor XIII.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4840-4844(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM SHORT).
RC TISSUE=Reticulocyte;
RX PubMed=2300550; DOI=10.1073/pnas.87.2.613;
RA Korsgren C., Lawler J., Lambert S., Speicher D., Cohen C.M.;
RT "Complete amino acid sequence and homologies of human erythrocyte membrane
RT protein band 4.2.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:613-617(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Reticulocyte;
RX PubMed=1689063; DOI=10.1073/pnas.87.3.955;
RA Sung L.A., Chien S., Chang L.-S., Lambert K., Bliss S.A., Bouhassira E.E.,
RA Nagel R.L., Schwartz R.S., Rybicki A.C.;
RT "Molecular cloning of human protein 4.2: a major component of the
RT erythrocyte membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:955-959(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT AND 3).
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 [7]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=1544941; DOI=10.1016/s0021-9258(18)42820-7;
RA Risinger M.A., Dotimas E.M., Cohen C.M.;
RT "Human erythrocyte protein 4.2, a high copy number membrane protein, is N-
RT myristylated.";
RL J. Biol. Chem. 267:5680-5685(1992).
RN [8]
RP PHOSPHORYLATION AT SER-248.
RX PubMed=8499466; DOI=10.1016/0005-2736(93)90156-t;
RA Dotimas E., Speicher D.W., Guptaroy B., Cohen C.M.;
RT "Structural domain mapping and phosphorylation of human erythrocyte
RT pallidin (band 4.2).";
RL Biochim. Biophys. Acta 1148:19-29(1993).
RN [9] {ECO:0007744|PDB:7UZS, ECO:0007744|PDB:7V0K, ECO:0007744|PDB:7V0Q, ECO:0007744|PDB:8CS9, ECO:0007744|PDB:8CSL, ECO:0007744|PDB:8CSW, ECO:0007744|PDB:8CTE}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.20 ANGSTROMS), FUNCTION, SUBUNIT,
RP ANKYRIN-1 COMPLEX IDENTIFICATION, AND INTERACTION WITH SLC4A1; AQP1 AND
RP ANK1.
RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w;
RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T.,
RA Clarke O.B.;
RT "Architecture of the human erythrocyte ankyrin-1 complex.";
RL Nat. Struct. Mol. Biol. 29:706-718(2022).
RN [10]
RP VARIANT SPH5 THR-112.
RX PubMed=1558976;
RA Bouhassira E.E., Schwartz R.S., Yawata Y., Ata K., Kanzaki A., Qiu J.J.-H.,
RA Nagel R.L., Rybicki A.C.;
RT "An alanine-to-threonine substitution in protein 4.2 cDNA is associated
RT with a Japanese form of hereditary hemolytic anemia (protein 4.2 Nippon).";
RL Blood 79:1846-1854(1992).
RN [11]
RP VARIANT SPH5 THR-112.
RX PubMed=7819064; DOI=10.1111/j.1365-2141.1994.tb05069.x;
RA Takaoka Y., Ideguchi H., Matsuda M., Sakamoto N., Takeuchi T., Fukumaki Y.;
RT "A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients
RT with hereditary spherocytosis (protein 4.2 Fukuoka).";
RL Br. J. Haematol. 88:527-533(1994).
RN [12]
RP VARIANT SPH5 GLN-280.
RX PubMed=7772513; DOI=10.1111/j.1365-2141.1995.tb08413.x;
RA Hayette S., Morle L., Bozon M., Ghanem A., Risinger M., Korsgren C.,
RA Tanner M.J.A., Fattoum S., Cohen C.M., Delaunay J.;
RT "A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated
RT with hereditary haemolytic anaemia.";
RL Br. J. Haematol. 89:762-770(1995).
RN [13]
RP VARIANTS SPH5 THR-112 AND CYS-287.
RX PubMed=8547071; DOI=10.1111/j.1365-2141.1995.tb05299.x;
RA Kanzaki A., Yasunaga M., Okamoto N., Inoue T., Yawata A., Wada H.,
RA Andoh A., Hodohara K., Fujiyama Y., Bamba T., Harano T., Harano K.,
RA Yawata Y.;
RT "Band 4.2 Shiga: 317 CGC-->TGC in compound heterozygotes with 142 GCT-->ACT
RT results in band 4.2 deficiency and microspherocytosis.";
RL Br. J. Haematol. 91:333-340(1995).
RN [14]
RP VARIANT SPH5 TYR-145.
RX PubMed=8547605; DOI=10.1016/0925-5710(95)00372-y;
RA Kanzaki A., Yawata Y., Yawata A., Inoue T., Okamoto N., Wada H., Harano T.,
RA Harano K., Wilmotte R., Hayette S., Nakamura Y., Niki T., Kawamura Y.,
RA Nakamura S., Matsuda T.;
RT "Band 4.2 Komatsu: 523 GAT-->TAT (175 Asp-->Tyr) in exon 4 of the band 4.2
RT gene associated with total deficiency of band 4.2, hemolytic anemia with
RT ovalostomatocytosis and marked disruption of the cytoskeletal network.";
RL Int. J. Hematol. 61:165-178(1995).
RN [15]
RP VARIANT SPH5 THR-112.
RX PubMed=10406914;
RA Perrotta S., Iolascon A., Polito R., d'Urzo G., Conte M.L.,
RA Miraglia del Giudice E.;
RT "4.2 Nippon mutation in a non-Japanese patient with hereditary
RT spherocytosis.";
RL Haematologica 84:660-662(1999).
CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex
CC involved in the stability and shape of the erythrocyte membrane.
CC {ECO:0000269|PubMed:35835865}.
CC -!- SUBUNIT: Component of the ankyrin-1 complex in the erythrocyte,
CC composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1
CC (PubMed:35835865). Interacts with SLC4A1 (via the cytoplasmic domain);
CC this interaction is mediated by the SLC4A1 Band 3-I dimer
CC (PubMed:35835865). Interacts with ANK1 (via ANK 1-13 repeats)
CC (PubMed:35835865). Interacts with AQP1 (via the C-terminal)
CC (PubMed:35835865). {ECO:0000269|PubMed:35835865}.
CC -!- INTERACTION:
CC P16452; Q92876: KLK6; NbExp=3; IntAct=EBI-1182496, EBI-2432309;
CC P16452; P58062: SPINK7; NbExp=3; IntAct=EBI-1182496, EBI-1182445;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of erythrocyte
CC membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Short;
CC IsoId=P16452-1; Sequence=Displayed;
CC Name=Long;
CC IsoId=P16452-2; Sequence=VSP_006416;
CC Name=3;
CC IsoId=P16452-3; Sequence=VSP_055340;
CC -!- PTM: Both cAMP-dependent kinase (CAPK) and another kinase present in
CC the red-blood cells seem to be able to phosphorylate EPB42.
CC {ECO:0000269|PubMed:8499466}.
CC -!- DISEASE: Spherocytosis 5 (SPH5) [MIM:612690]: Spherocytosis is a
CC hematologic disorder leading to chronic hemolytic anemia and
CC characterized by numerous abnormally shaped erythrocytes which are
CC generally spheroidal. Absence of band 4.2 associated with spur or
CC target erythrocytes has also been reported.
CC {ECO:0000269|PubMed:10406914, ECO:0000269|PubMed:1558976,
CC ECO:0000269|PubMed:7772513, ECO:0000269|PubMed:7819064,
CC ECO:0000269|PubMed:8547071, ECO:0000269|PubMed:8547605}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The substitution of an Ala for a Cys in the active site
CC may be responsible for the lack of transglutaminase activity of band
CC 4.2.
CC -!- MISCELLANEOUS: [Isoform Short]: Major isoform.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36401.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA36402.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M60298; AAA74589.1; -; mRNA.
DR EMBL; L06519; AAA52385.1; -; Genomic_DNA.
DR EMBL; L06447; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06448; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06449; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06450; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06511; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06512; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06513; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06515; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06516; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06517; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; L06518; AAA52385.1; JOINED; Genomic_DNA.
DR EMBL; M29399; AAA35798.1; -; mRNA.
DR EMBL; M30647; AAA36401.1; ALT_FRAME; mRNA.
DR EMBL; M30646; AAA36402.1; ALT_FRAME; mRNA.
DR EMBL; AC068724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92591.1; -; Genomic_DNA.
DR EMBL; BC096093; AAH96093.1; -; mRNA.
DR EMBL; BC096094; AAH96094.1; -; mRNA.
DR EMBL; BC099627; AAH99627.1; -; mRNA.
DR CCDS; CCDS10093.1; -. [P16452-2]
DR CCDS; CCDS45249.1; -. [P16452-1]
DR PIR; A39707; A39707.
DR RefSeq; NP_000110.2; NM_000119.2. [P16452-2]
DR RefSeq; NP_001107606.1; NM_001114134.1. [P16452-1]
DR RefSeq; XP_011519651.1; XM_011521349.2.
DR RefSeq; XP_011519652.1; XM_011521350.2. [P16452-2]
DR RefSeq; XP_011519653.1; XM_011521351.2. [P16452-2]
DR PDB; 7TVZ; EM; 3.60 A; E=1-691.
DR PDB; 7TW0; EM; 4.60 A; E=1-691.
DR PDB; 7TW1; EM; 4.60 A; E/F=1-691.
DR PDB; 7TW3; EM; 4.40 A; E=1-691.
DR PDB; 7TW5; EM; 5.70 A; E=1-691.
DR PDB; 7TW6; EM; 5.60 A; E=1-691.
DR PDB; 7UZS; EM; 2.20 A; X=1-691.
DR PDB; 7V0K; EM; 2.40 A; X=1-691.
DR PDB; 7V0Q; EM; 2.50 A; X=1-691.
DR PDB; 8CS9; EM; 2.74 A; X=1-691.
DR PDB; 8CSL; EM; 25.00 A; X=1-691.
DR PDB; 8CSW; EM; 2.50 A; X=1-691.
DR PDB; 8CTE; EM; 2.90 A; X=1-691.
DR PDBsum; 7TVZ; -.
DR PDBsum; 7TW0; -.
DR PDBsum; 7TW1; -.
DR PDBsum; 7TW3; -.
DR PDBsum; 7TW5; -.
DR PDBsum; 7TW6; -.
DR PDBsum; 7UZS; -.
DR PDBsum; 7V0K; -.
DR PDBsum; 7V0Q; -.
DR PDBsum; 8CS9; -.
DR PDBsum; 8CSL; -.
DR PDBsum; 8CSW; -.
DR PDBsum; 8CTE; -.
DR AlphaFoldDB; P16452; -.
DR EMDB; EMD-26142; -.
DR EMDB; EMD-26146; -.
DR EMDB; EMD-26147; -.
DR EMDB; EMD-26149; -.
DR EMDB; EMD-26151; -.
DR EMDB; EMD-26153; -.
DR EMDB; EMD-26154; -.
DR EMDB; EMD-26917; -.
DR EMDB; EMD-26943; -.
DR EMDB; EMD-26948; -.
DR EMDB; EMD-26960; -.
DR EMDB; EMD-26965; -.
DR EMDB; EMD-26973; -.
DR EMDB; EMD-26988; -.
DR SMR; P16452; -.
DR BioGRID; 108352; 35.
DR IntAct; P16452; 9.
DR STRING; 9606.ENSP00000497777; -.
DR GlyConnect; 2894; 1 O-GlcNAc glycan (1 site).
DR GlyCosmos; P16452; 1 site, 1 glycan.
DR GlyGen; P16452; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P16452; -.
DR PhosphoSitePlus; P16452; -.
DR BioMuta; EPB42; -.
DR DMDM; 215274164; -.
DR jPOST; P16452; -.
DR MassIVE; P16452; -.
DR PaxDb; 9606-ENSP00000300215; -.
DR PeptideAtlas; P16452; -.
DR ProteomicsDB; 53363; -. [P16452-1]
DR ProteomicsDB; 53364; -. [P16452-2]
DR ProteomicsDB; 62192; -.
DR Antibodypedia; 11125; 131 antibodies from 19 providers.
DR DNASU; 2038; -.
DR Ensembl; ENST00000441366.7; ENSP00000396616.2; ENSG00000166947.15. [P16452-1]
DR Ensembl; ENST00000648595.1; ENSP00000497777.1; ENSG00000166947.15. [P16452-2]
DR GeneID; 2038; -.
DR KEGG; hsa:2038; -.
DR MANE-Select; ENST00000441366.7; ENSP00000396616.2; NM_001114134.2; NP_001107606.1.
DR UCSC; uc001zra.5; human. [P16452-1]
DR AGR; HGNC:3381; -.
DR CTD; 2038; -.
DR DisGeNET; 2038; -.
DR GeneCards; EPB42; -.
DR GeneReviews; EPB42; -.
DR HGNC; HGNC:3381; EPB42.
DR HPA; ENSG00000166947; Tissue enriched (bone).
DR MalaCards; EPB42; -.
DR MIM; 177070; gene.
DR MIM; 612690; phenotype.
DR neXtProt; NX_P16452; -.
DR OpenTargets; ENSG00000166947; -.
DR Orphanet; 822; Hereditary spherocytosis.
DR PharmGKB; PA27814; -.
DR VEuPathDB; HostDB:ENSG00000166947; -.
DR eggNOG; ENOG502R9T9; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_3_0_1; -.
DR InParanoid; P16452; -.
DR OMA; NPWGRED; -.
DR OrthoDB; 5344745at2759; -.
DR PhylomeDB; P16452; -.
DR TreeFam; TF324278; -.
DR BRENDA; 2.3.2.13; 2681.
DR PathwayCommons; P16452; -.
DR SignaLink; P16452; -.
DR SIGNOR; P16452; -.
DR BioGRID-ORCS; 2038; 9 hits in 1148 CRISPR screens.
DR ChiTaRS; EPB42; human.
DR GeneWiki; Protein_4.2; -.
DR GenomeRNAi; 2038; -.
DR Pharos; P16452; Tbio.
DR PRO; PR:P16452; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P16452; Protein.
DR Bgee; ENSG00000166947; Expressed in blood and 71 other cell types or tissues.
DR ExpressionAtlas; P16452; baseline and differential.
DR Genevisible; P16452; HS.
DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
DR GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR PANTHER; PTHR11590:SF44; PROTEIN 4.2; 1.
DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell shape; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease variant;
KW Erythrocyte maturation; Hereditary hemolytic anemia; Lipoprotein; Membrane;
KW Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..691
FT /note="Protein 4.2"
FT /id="PRO_0000213720"
FT REGION 31..39
FT /note="Band 3 binding"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000305|PubMed:8499466"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:1544941"
FT VAR_SEQ 3
FT /note="Q -> QGEPSQRSTGLAGLYAAPAASPVFIKGSGMD (in isoform
FT Long)"
FT /evidence="ECO:0000303|PubMed:1689063,
FT ECO:0000303|PubMed:2052563"
FT /id="VSP_006416"
FT VAR_SEQ 324..395
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055340"
FT VARIANT 112
FT /note="A -> T (in SPH5; Nippon/Fukuoka; dbSNP:rs104894487)"
FT /evidence="ECO:0000269|PubMed:10406914,
FT ECO:0000269|PubMed:1558976, ECO:0000269|PubMed:7819064,
FT ECO:0000269|PubMed:8547071"
FT /id="VAR_007482"
FT VARIANT 145
FT /note="D -> Y (in SPH5; Komatsu; dbSNP:rs143682977)"
FT /evidence="ECO:0000269|PubMed:8547605"
FT /id="VAR_058099"
FT VARIANT 280
FT /note="R -> Q (in SPH5; Tozeur; dbSNP:rs121917734)"
FT /evidence="ECO:0000269|PubMed:7772513"
FT /id="VAR_012268"
FT VARIANT 287
FT /note="R -> C (in SPH5; Shiga; dbSNP:rs515726212)"
FT /evidence="ECO:0000269|PubMed:8547071"
FT /id="VAR_058100"
FT CONFLICT 350
FT /note="H -> D (in Ref. 1; AAA74589/AAA52385 and 2;
FT AAA35798)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="L -> V (in Ref. 1; AAA74589/AAA52385 and 2;
FT AAA35798)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:7UZS"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:7UZS"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 320..334
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 442..458
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 490..499
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 505..517
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 522..535
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 540..548
FT /evidence="ECO:0007829|PDB:7UZS"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 560..570
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 576..586
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:7UZS"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 631..638
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 660..669
FT /evidence="ECO:0007829|PDB:7UZS"
FT STRAND 676..685
FT /evidence="ECO:0007829|PDB:7UZS"
SQ SEQUENCE 691 AA; 77009 MW; 38225C311E478580 CRC64;
MGQALGIKSC DFQAARNNEE HHTKALSSRR LFVRRGQPFT IILYFRAPVR AFLPALKKVA
LTAQTGEQPS KINRTQATFP ISSLGDRKWW SAVVEERDAQ SWTISVTTPA DAVIGHYSLL
LQVSGRKQLL LGQFTLLFNP WNREDAVFLK NEAQRMEYLL NQNGLIYLGT ADCIQAESWD
FGQFEGDVID LSLRLLSKDK QVEKWSQPVH VARVLGALLH FLKEQRVLPT PQTQATQEGA
LLNKRRGSVP ILRQWLTGRG RPVYDGQAWV LAAVACTVLR CLGIPARVVT TFASAQGTGG
RLLIDEYYNE EGLQNGEGQR GRIWIFQTST ECWMTRPALP QGYDGWQILH PSAPNGGGVL
GSCDLVPVRA VKEGTLGLTP AVSDLFAAIN ASCVVWKCCE DGTLELTDSN TKYVGNNIST
KGVGSDRCED ITQNYKYPEG SLQEKEVLER VEKEKMEREK DNGIRPPSLE TASPLYLLLK
APSSLPLRGD AQISVTLVNH SEQEKAVQLA IGVQAVHYNG VLAAKLWRKK LHLTLSANLE
KIITIGLFFS NFERNPPENT FLRLTAMATH SESNLSCFAQ EDIAICRPHL AIKMPEKAEQ
YQPLTASVSL QNSLDAPMED CVISILGRGL IHRERSYRFR SVWPENTMCA KFQFTPTHVG
LQRLTVEVDC NMFQNLTNYK SVTVVAPELS A
//
