KREM1_HUMAN
ID KREM1_HUMAN Reviewed; 473 AA.
AC Q96MU8; B0QY46; B0QY47; B1AJR5; Q5TIB9; Q6P3X6; Q9BY70; Q9UGS5; Q9UGU1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Kremen protein 1;
DE AltName: Full=Dickkopf receptor;
DE AltName: Full=Kringle domain-containing transmembrane protein 1;
DE AltName: Full=Kringle-containing protein marking the eye and the nose;
DE Flags: Precursor;
GN Name=KREMEN1; Synonyms=KREMEN, KRM1;
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 1).
RA Nakamura T., Nakamura T.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
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 [6]
RP INTERACTION WITH LRP6; DKK1 AND RSPO1.
RX PubMed=17804805; DOI=10.1073/pnas.0702305104;
RA Binnerts M.E., Kim K.A., Bright J.M., Patel S.M., Tran K., Zhou M.,
RA Leung J.M., Liu Y., Lomas W.E. III, Dixon M., Hazell S.A., Wagle M.,
RA Nie W.S., Tomasevic N., Williams J., Zhan X., Levy M.D., Funk W.D., Abo A.;
RT "R-Spondin1 regulates Wnt signaling by inhibiting internalization of
RT LRP6.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14700-14705(2007).
RN [7]
RP INVOLVEMENT IN ECTD13, AND VARIANT ECTD13 SER-207.
RX PubMed=27049303; DOI=10.1038/ejhg.2016.29;
RA Issa Y.A., Kamal L., Rayyan A.A., Dweik D., Pierce S., Lee M.K., King M.C.,
RA Walsh T., Kanaan M.;
RT "Mutation of KREMEN1, a modulator of Wnt signaling, is responsible for
RT ectodermal dysplasia including oligodontia in Palestinian families.";
RL Eur. J. Hum. Genet. 24:1430-1435(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 29-373, DISULFIDE BOND, AND
RP IDENTIFICATION IN A TERNARY COMPLEX WITH DKK1 AND LRP6.
RX PubMed=27524201; DOI=10.1016/j.str.2016.06.020;
RA Zebisch M., Jackson V.A., Zhao Y., Jones E.Y.;
RT "Structure of the dual-mode wnt regulator Kremen1 and insight into ternary
RT complex formation with LRP6 and Dickkopf.";
RL Structure 24:1599-1605(2016).
CC -!- FUNCTION: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to
CC inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt
CC receptors LRP5 and LRP6. In the absence of DKK1, potentiates Wnt-beta-
CC catenin signaling by maintaining LRP5 or LRP6 at the cell membrane. Can
CC trigger apoptosis in a Wnt-independent manner and this apoptotic
CC activity is inhibited upon binding of the ligand DKK1. Plays a role in
CC limb development; attenuates Wnt signaling in the developing limb to
CC allow normal limb patterning and can also negatively regulate bone
CC formation. Modulates cell fate decisions in the developing cochlea with
CC an inhibitory role in hair cell fate specification.
CC {ECO:0000250|UniProtKB:Q90Y90, ECO:0000250|UniProtKB:Q99N43}.
CC -!- SUBUNIT: Forms a ternary complex with DKK1 and LRP6 (PubMed:27524201).
CC Interacts with LRP6 in a DKK1-dependent manner. Interacts with DKK1 and
CC RSPO1 (via FU repeats) (PubMed:17804805). {ECO:0000269|PubMed:17804805,
CC ECO:0000269|PubMed:27524201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99N43};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96MU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MU8-2; Sequence=VSP_034914, VSP_003900;
CC Name=3;
CC IsoId=Q96MU8-3; Sequence=VSP_034914, VSP_015698;
CC -!- DISEASE: Ectodermal dysplasia 13, hair/tooth type (ECTD13)
CC [MIM:617392]: A form of ectodermal dysplasia, a disorder due to
CC abnormal development of two or more ectodermal structures. ECTD13 is an
CC autosomal recessive form characterized by severe oligodontia
CC accompanied by anomalies of hair and skin.
CC {ECO:0000269|PubMed:27049303}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Exon 1 splicing donor site is not
CC canonical.
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DR EMBL; AB059618; BAB40969.1; -; mRNA.
DR EMBL; AK056425; BAB71180.1; -; mRNA.
DR EMBL; AL021393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59774.1; -; Genomic_DNA.
DR EMBL; BC063787; AAH63787.1; -; mRNA.
DR CCDS; CCDS13849.1; -. [Q96MU8-2]
DR CCDS; CCDS43000.2; -. [Q96MU8-3]
DR RefSeq; NP_001034659.2; NM_001039570.2. [Q96MU8-3]
DR RefSeq; NP_114434.3; NM_032045.4. [Q96MU8-2]
DR PDB; 5FWS; X-ray; 1.90 A; A=29-373.
DR PDB; 5FWT; X-ray; 2.10 A; A=29-373.
DR PDB; 5FWU; X-ray; 2.80 A; A=29-373.
DR PDB; 5FWV; X-ray; 3.20 A; A=29-373.
DR PDB; 5FWW; X-ray; 3.50 A; B=30-322.
DR PDB; 7BZT; EM; 3.00 A; E=23-375.
DR PDB; 7BZU; EM; 3.00 A; E=23-375.
DR PDBsum; 5FWS; -.
DR PDBsum; 5FWT; -.
DR PDBsum; 5FWU; -.
DR PDBsum; 5FWV; -.
DR PDBsum; 5FWW; -.
DR PDBsum; 7BZT; -.
DR PDBsum; 7BZU; -.
DR AlphaFoldDB; Q96MU8; -.
DR SMR; Q96MU8; -.
DR BioGRID; 123844; 1.
DR CORUM; Q96MU8; -.
DR DIP; DIP-46462N; -.
DR IntAct; Q96MU8; 3.
DR STRING; 9606.ENSP00000331242; -.
DR GlyGen; Q96MU8; 6 sites.
DR iPTMnet; Q96MU8; -.
DR PhosphoSitePlus; Q96MU8; -.
DR BioMuta; KREMEN1; -.
DR DMDM; 212287927; -.
DR jPOST; Q96MU8; -.
DR MassIVE; Q96MU8; -.
DR PaxDb; Q96MU8; -.
DR PeptideAtlas; Q96MU8; -.
DR PRIDE; Q96MU8; -.
DR ProteomicsDB; 77415; -. [Q96MU8-1]
DR ProteomicsDB; 77416; -. [Q96MU8-2]
DR ProteomicsDB; 77417; -. [Q96MU8-3]
DR Antibodypedia; 24417; 323 antibodies from 28 providers.
DR DNASU; 83999; -.
DR Ensembl; ENST00000327813.9; ENSP00000331242.5; ENSG00000183762.13. [Q96MU8-2]
DR Ensembl; ENST00000400335.9; ENSP00000383189.4; ENSG00000183762.13. [Q96MU8-3]
DR Ensembl; ENST00000407188.5; ENSP00000385431.1; ENSG00000183762.13. [Q96MU8-1]
DR GeneID; 83999; -.
DR KEGG; hsa:83999; -.
DR MANE-Select; ENST00000400335.9; ENSP00000383189.4; NM_001039570.3; NP_001034659.2. [Q96MU8-3]
DR UCSC; uc003ael.3; human. [Q96MU8-1]
DR CTD; 83999; -.
DR DisGeNET; 83999; -.
DR GeneCards; KREMEN1; -.
DR HGNC; HGNC:17550; KREMEN1.
DR HPA; ENSG00000183762; Low tissue specificity.
DR MalaCards; KREMEN1; -.
DR MIM; 609898; gene.
DR MIM; 617392; phenotype.
DR neXtProt; NX_Q96MU8; -.
DR OpenTargets; ENSG00000183762; -.
DR PharmGKB; PA38241; -.
DR VEuPathDB; HostDB:ENSG00000183762; -.
DR eggNOG; KOG4157; Eukaryota.
DR GeneTree; ENSGT00940000158390; -.
DR HOGENOM; CLU_043485_0_0_1; -.
DR InParanoid; Q96MU8; -.
DR OMA; DNVHQNK; -.
DR OrthoDB; 516719at2759; -.
DR PhylomeDB; Q96MU8; -.
DR TreeFam; TF331319; -.
DR PathwayCommons; Q96MU8; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR Reactome; R-HSA-5339717; Signaling by LRP5 mutants.
DR SignaLink; Q96MU8; -.
DR SIGNOR; Q96MU8; -.
DR BioGRID-ORCS; 83999; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; KREMEN1; human.
DR GeneWiki; KREMEN1; -.
DR GenomeRNAi; 83999; -.
DR Pharos; Q96MU8; Tbio.
DR PRO; PR:Q96MU8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96MU8; protein.
DR Bgee; ENSG00000183762; Expressed in upper arm skin and 182 other tissues.
DR ExpressionAtlas; Q96MU8; baseline and differential.
DR Genevisible; Q96MU8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0007154; P:cell communication; TAS:UniProtKB.
DR GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; NAS:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR017076; Kremen.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF01822; WSC; 1.
DR PIRSF; PIRSF036961; Kremen; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS51212; WSC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Ectodermal dysplasia; Glycoprotein; Kringle; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..473
FT /note="Kremen protein 1"
FT /id="PRO_0000021564"
FT TOPO_DOM 21..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..114
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 116..210
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 214..321
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 414..473
FT /note="Essential for apoptotic activity"
FT /evidence="ECO:0000250|UniProtKB:Q99N43"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..114
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 55..95
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 84..109
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 122..186
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 147..167
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 151..169
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 190..198
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT DISULFID 214..240
FT /evidence="ECO:0000269|PubMed:27524201,
FT ECO:0007744|PDB:5FWS, ECO:0007744|PDB:5FWT,
FT ECO:0007744|PDB:5FWU, ECO:0007744|PDB:5FWV,
FT ECO:0007744|PDB:5FWW"
FT VAR_SEQ 31
FT /note="E -> GPE (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_034914"
FT VAR_SEQ 373..389
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015698"
FT VAR_SEQ 471..473
FT /note="VSD -> AIQDSEVTSLIWSQGQPRSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003900"
FT VARIANT 207
FT /note="F -> S (in ECTD13; dbSNP:rs1057524917)"
FT /evidence="ECO:0000269|PubMed:27049303"
FT /id="VAR_078807"
FT CONFLICT 204
FT /note="I -> V (in Ref. 2; BAB71180)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5FWW"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7BZT"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5FWT"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7BZT"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5FWS"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7BZT"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5FWS"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5FWS"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5FWS"
FT TURN 173..178
FT /evidence="ECO:0007829|PDB:5FWS"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5FWS"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:5FWS"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:5FWS"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:5FWS"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:5FWS"
SQ SEQUENCE 473 AA; 51744 MW; F6D30DDE708C186B CRC64;
MAPPAARLAL LSAAALTLAA RPAPSPGLGP ECFTANGADY RGTQNWTALQ GGKPCLFWNE
TFQHPYNTLK YPNGEGGLGE HNYCRNPDGD VSPWCYVAEH EDGVYWKYCE IPACQMPGNL
GCYKDHGNPP PLTGTSKTSN KLTIQTCISF CRSQRFKFAG MESGYACFCG NNPDYWKYGE
AASTECNSVC FGDHTQPCGG DGRIILFDTL VGACGGNYSA MSSVVYSPDF PDTYATGRVC
YWTIRVPGAS HIHFSFPLFD IRDSADMVEL LDGYTHRVLA RFHGRSRPPL SFNVSLDFVI
LYFFSDRINQ AQGFAVLYQA VKEELPQERP AVNQTVAEVI TEQANLSVSA ARSSKVLYVI
TTSPSHPPQT VPGSNSWAPP MGAGSHRVEG WTVYGLATLL ILTVTAIVAK ILLHVTFKSH
RVPASGDLRD CHQPGTSGEI WSIFYKPSTS ISIFKKKLKG QSQQDDRNPL VSD
