SCMH1_HUMAN
ID SCMH1_HUMAN Reviewed; 660 AA.
AC Q96GD3; B4DRQ8; Q5VT76; Q6IAJ4; Q8WU48; Q9UKM5; Q9UKM6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Polycomb protein SCMH1;
DE AltName: Full=Sex comb on midleg homolog 1;
GN Name=SCMH1 {ECO:0000312|EMBL:CAH72793.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF01150.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), AND TISSUE SPECIFICITY.
RC TISSUE=Heart {ECO:0000312|EMBL:AAF01150.1}, and
RC Skeletal muscle {ECO:0000269|PubMed:10524249};
RX PubMed=10524249; DOI=10.1016/s0378-1119(99)00285-1;
RA Berger J., Kurahashi H., Takihara Y., Shimada K., Brock H.W., Randazzo F.;
RT "The human homolog of Sex comb on midleg (SCMH1) maps to chromosome 1p34.";
RL Gene 237:185-191(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Tongue;
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] {ECO:0000305, ECO:0000312|EMBL:CAG33442.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Fetal brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH21252.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye {ECO:0000312|EMBL:AAH21252.1}, and
RC Muscle {ECO:0000312|EMBL:AAH09752.1};
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 IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH A PRC1-LIKE
RP COMPLEX.
RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002;
RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA Kingston R.E.;
RT "The core of the polycomb repressive complex is compositionally and
RT functionally conserved in flies and humans.";
RL Mol. Cell. Biol. 22:6070-6078(2002).
CC -!- FUNCTION: Associates with Polycomb group (PcG) multiprotein complexes;
CC the complex class is required to maintain the transcriptionally
CC repressive state of some genes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SAM domain of PHC1 via its SAM domain in
CC vitro (By similarity). Associates with a PRC1-like complex.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q96GD3; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-713793, EBI-744820;
CC Q96GD3; P43365: MAGEA12; NbExp=3; IntAct=EBI-713793, EBI-749530;
CC Q96GD3; Q9UHJ3: SFMBT1; NbExp=3; IntAct=EBI-713793, EBI-747398;
CC Q96GD3; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-713793, EBI-12025260;
CC Q96GD3; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-713793, EBI-741480;
CC Q96GD3; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-713793, EBI-10173939;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96GD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GD3-2; Sequence=VSP_051676, VSP_051679;
CC Name=3;
CC IsoId=Q96GD3-3; Sequence=VSP_051678;
CC Name=4 {ECO:0000269|PubMed:10524249};
CC IsoId=Q96GD3-4; Sequence=VSP_051677, VSP_051679;
CC Name=5 {ECO:0000269|PubMed:10524249};
CC IsoId=Q96GD3-5; Sequence=VSP_051678, VSP_051679;
CC Name=6;
CC IsoId=Q96GD3-6; Sequence=VSP_051677, VSP_043395, VSP_051679;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, muscle and pancreas.
CC Weakly expressed in brain, placenta, lung, liver and kidney.
CC {ECO:0000269|PubMed:10524249}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention.
CC {ECO:0000303|PubMed:10524249}.
CC -!- SIMILARITY: Belongs to the SCM family. {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; AF149045; AAF01150.1; -; mRNA.
DR EMBL; AF149046; AAF01151.1; -; mRNA.
DR EMBL; AK299383; BAG61370.1; -; mRNA.
DR EMBL; CR457161; CAG33442.1; -; mRNA.
DR EMBL; BX640721; CAE45840.1; -; mRNA.
DR EMBL; AL110502; CAI22109.1; -; Genomic_DNA.
DR EMBL; AL391730; CAI22109.1; JOINED; Genomic_DNA.
DR EMBL; AL110502; CAI22110.1; -; Genomic_DNA.
DR EMBL; AL391730; CAI22110.1; JOINED; Genomic_DNA.
DR EMBL; AL110502; CAI22111.1; -; Genomic_DNA.
DR EMBL; AL391730; CAI22111.1; JOINED; Genomic_DNA.
DR EMBL; AL606484; CAI22111.1; JOINED; Genomic_DNA.
DR EMBL; AL110502; CAI22112.1; -; Genomic_DNA.
DR EMBL; AL391730; CAI22112.1; JOINED; Genomic_DNA.
DR EMBL; AL110502; CAI22113.1; -; Genomic_DNA.
DR EMBL; AL391730; CAI22113.1; JOINED; Genomic_DNA.
DR EMBL; AL391730; CAH72791.1; -; Genomic_DNA.
DR EMBL; AL110502; CAH72791.1; JOINED; Genomic_DNA.
DR EMBL; AL391730; CAH72793.1; -; Genomic_DNA.
DR EMBL; AL110502; CAH72793.1; JOINED; Genomic_DNA.
DR EMBL; AL391730; CAH72794.1; -; Genomic_DNA.
DR EMBL; AL110502; CAH72794.1; JOINED; Genomic_DNA.
DR EMBL; AL606484; CAH72794.1; JOINED; Genomic_DNA.
DR EMBL; AL391730; CAH72795.1; -; Genomic_DNA.
DR EMBL; AL110502; CAH72795.1; JOINED; Genomic_DNA.
DR EMBL; AL391730; CAH72796.1; -; Genomic_DNA.
DR EMBL; AL110502; CAH72796.1; JOINED; Genomic_DNA.
DR EMBL; AL606484; CAH72242.1; -; Genomic_DNA.
DR EMBL; AL110502; CAH72242.1; JOINED; Genomic_DNA.
DR EMBL; AL391730; CAH72242.1; JOINED; Genomic_DNA.
DR EMBL; BC009752; AAH09752.1; -; mRNA.
DR EMBL; BC021252; AAH21252.1; -; mRNA.
DR CCDS; CCDS30688.1; -. [Q96GD3-1]
DR CCDS; CCDS461.1; -. [Q96GD3-4]
DR CCDS; CCDS53301.1; -. [Q96GD3-5]
DR CCDS; CCDS53302.1; -. [Q96GD3-3]
DR CCDS; CCDS53303.1; -. [Q96GD3-6]
DR CCDS; CCDS53304.1; -. [Q96GD3-2]
DR RefSeq; NP_001026864.1; NM_001031694.2. [Q96GD3-1]
DR RefSeq; NP_001165689.1; NM_001172218.1. [Q96GD3-5]
DR RefSeq; NP_001165690.1; NM_001172219.1. [Q96GD3-2]
DR RefSeq; NP_001165691.1; NM_001172220.1. [Q96GD3-5]
DR RefSeq; NP_001165692.1; NM_001172221.1. [Q96GD3-3]
DR RefSeq; NP_001165693.1; NM_001172222.2. [Q96GD3-6]
DR RefSeq; NP_036368.1; NM_012236.3. [Q96GD3-4]
DR RefSeq; XP_006710527.1; XM_006710464.1. [Q96GD3-3]
DR RefSeq; XP_011539335.1; XM_011541033.2. [Q96GD3-1]
DR RefSeq; XP_011539338.1; XM_011541036.2. [Q96GD3-3]
DR RefSeq; XP_016856188.1; XM_017000699.1. [Q96GD3-3]
DR RefSeq; XP_016856196.1; XM_017000707.1.
DR PDB; 2P0K; X-ray; 1.75 A; A=27-238.
DR PDBsum; 2P0K; -.
DR AlphaFoldDB; Q96GD3; -.
DR SMR; Q96GD3; -.
DR BioGRID; 116609; 53.
DR CORUM; Q96GD3; -.
DR IntAct; Q96GD3; 45.
DR MINT; Q96GD3; -.
DR STRING; 9606.ENSP00000318094; -.
DR DrugBank; DB03345; Mercaptoethanol.
DR iPTMnet; Q96GD3; -.
DR PhosphoSitePlus; Q96GD3; -.
DR BioMuta; SCMH1; -.
DR DMDM; 60390956; -.
DR EPD; Q96GD3; -.
DR jPOST; Q96GD3; -.
DR MassIVE; Q96GD3; -.
DR MaxQB; Q96GD3; -.
DR PaxDb; Q96GD3; -.
DR PeptideAtlas; Q96GD3; -.
DR PRIDE; Q96GD3; -.
DR ProteomicsDB; 76617; -. [Q96GD3-1]
DR ProteomicsDB; 76618; -. [Q96GD3-2]
DR ProteomicsDB; 76619; -. [Q96GD3-3]
DR ProteomicsDB; 76620; -. [Q96GD3-4]
DR ProteomicsDB; 76621; -. [Q96GD3-5]
DR ProteomicsDB; 76622; -. [Q96GD3-6]
DR ABCD; Q96GD3; 1 sequenced antibody.
DR Antibodypedia; 32169; 230 antibodies from 24 providers.
DR DNASU; 22955; -.
DR Ensembl; ENST00000326197.11; ENSP00000318094.7; ENSG00000010803.16. [Q96GD3-1]
DR Ensembl; ENST00000337495.9; ENSP00000337352.5; ENSG00000010803.16. [Q96GD3-2]
DR Ensembl; ENST00000361191.9; ENSP00000354656.5; ENSG00000010803.16. [Q96GD3-5]
DR Ensembl; ENST00000361705.7; ENSP00000354996.3; ENSG00000010803.16. [Q96GD3-4]
DR Ensembl; ENST00000372595.5; ENSP00000361676.1; ENSG00000010803.16. [Q96GD3-3]
DR Ensembl; ENST00000372596.5; ENSP00000361677.1; ENSG00000010803.16. [Q96GD3-5]
DR Ensembl; ENST00000372597.5; ENSP00000361678.1; ENSG00000010803.16. [Q96GD3-4]
DR Ensembl; ENST00000397171.6; ENSP00000380356.2; ENSG00000010803.16. [Q96GD3-5]
DR Ensembl; ENST00000397174.6; ENSP00000380359.3; ENSG00000010803.16. [Q96GD3-1]
DR Ensembl; ENST00000402904.6; ENSP00000386079.3; ENSG00000010803.16. [Q96GD3-3]
DR Ensembl; ENST00000456518.3; ENSP00000403974.2; ENSG00000010803.16. [Q96GD3-6]
DR GeneID; 22955; -.
DR KEGG; hsa:22955; -.
DR UCSC; uc001cgp.4; human. [Q96GD3-1]
DR CTD; 22955; -.
DR DisGeNET; 22955; -.
DR GeneCards; SCMH1; -.
DR HGNC; HGNC:19003; SCMH1.
DR HPA; ENSG00000010803; Low tissue specificity.
DR MIM; 616396; gene.
DR neXtProt; NX_Q96GD3; -.
DR OpenTargets; ENSG00000010803; -.
DR PharmGKB; PA134870272; -.
DR VEuPathDB; HostDB:ENSG00000010803; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000157999; -.
DR HOGENOM; CLU_015000_1_1_1; -.
DR InParanoid; Q96GD3; -.
DR OMA; AMFDREQ; -.
DR OrthoDB; 229086at2759; -.
DR PhylomeDB; Q96GD3; -.
DR TreeFam; TF106488; -.
DR PathwayCommons; Q96GD3; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence. [Q96GD3-2]
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. [Q96GD3-2]
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. [Q96GD3-2]
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. [Q96GD3-2]
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. [Q96GD3-2]
DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins. [Q96GD3-2]
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. [Q96GD3-2]
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. [Q96GD3-2]
DR SignaLink; Q96GD3; -.
DR BioGRID-ORCS; 22955; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; SCMH1; human.
DR EvolutionaryTrace; Q96GD3; -.
DR GeneWiki; SCMH1; -.
DR GenomeRNAi; 22955; -.
DR Pharos; Q96GD3; Tbio.
DR PRO; PR:Q96GD3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96GD3; protein.
DR Bgee; ENSG00000010803; Expressed in lower esophagus muscularis layer and 174 other tissues.
DR ExpressionAtlas; Q96GD3; baseline and differential.
DR Genevisible; Q96GD3; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.90.1150.190; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR033763; SCML2_RBR.
DR InterPro; IPR021987; SLED.
DR InterPro; IPR038348; SLED_sf.
DR Pfam; PF02820; MBT; 2.
DR Pfam; PF17208; RBR; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF12140; SLED; 1.
DR SMART; SM00561; MBT; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..660
FT /note="Polycomb protein SCMH1"
FT /id="PRO_0000114334"
FT REPEAT 28..126
FT /note="MBT 1"
FT REPEAT 134..235
FT /note="MBT 2"
FT DOMAIN 593..658
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 233..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10524249,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.3"
FT /id="VSP_051678"
FT VAR_SEQ 1..48
FT /note="MLVCYSVLACEILWDLPCSIMGSPLGHFTWDKYLKETCSVPAPVHCFK ->
FT M (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10524249,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_051677"
FT VAR_SEQ 1..24
FT /note="MLVCYSVLACEILWDLPCSIMGSP -> MQPNVIDWSDVRKHKYGHLSESAS
FT QYQEAADILD (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_051676"
FT VAR_SEQ 128..238
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043395"
FT VAR_SEQ 550..571
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:10524249,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005"
FT /id="VSP_051679"
FT CONFLICT 463
FT /note="F -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:2P0K"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 71..84
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2P0K"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:2P0K"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2P0K"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:2P0K"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2P0K"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:2P0K"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2P0K"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:2P0K"
SQ SEQUENCE 660 AA; 73354 MW; 6544DD484DA8D037 CRC64;
MLVCYSVLAC EILWDLPCSI MGSPLGHFTW DKYLKETCSV PAPVHCFKQS YTPPSNEFKI
SMKLEAQDPR NTTSTCIATV VGLTGARLRL RLDGSDNKND FWRLVDSAEI QPIGNCEKNG
GMLQPPLGFR LNASSWPMFL LKTLNGAEMA PIRIFHKEPP SPSHNFFKMG MKLEAVDRKN
PHFICPATIG EVRGSEVLVT FDGWRGAFDY WCRFDSRDIF PVGWCSLTGD NLQPPGTKVV
IPKNPYPASD VNTEKPSIHS STKTVLEHQP GQRGRKPGKK RGRTPKTLIS HPISAPSKTA
EPLKFPKKRG PKPGSKRKPR TLLNPPPASP TTSTPEPDTS TVPQDAATIP SSAMQAPTVC
IYLNKNGSTG PHLDKKKVQQ LPDHFGPARA SVVLQQAVQA CIDCAYHQKT VFSFLKQGHG
GEVISAVFDR EQHTLNLPAV NSITYVLRFL EKLCHNLRSD NLFGNQPFTQ THLSLTAIEY
SHSHDRYLPG ETFVLGNSLA RSLEPHSDSM DSASNPTNLV STSQRHRPLL SSCGLPPSTA
SAVRRLCSRG VLKGSNERRD MESFWKLNRS PGSDRYLESR DASRLSGRDP SSWTVEDVMQ
FVREADPQLG PHADLFRKHE IDGKALLLLR SDMMMKYMGL KLGPALKLSY HIDRLKQGKF
