CRBG1_HUMAN
ID CRBG1_HUMAN Reviewed; 1723 AA.
AC Q9Y4K1; B4DU04; O00296; Q5VWJ2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Beta/gamma crystallin domain-containing protein 1 {ECO:0000312|HGNC:HGNC:356};
DE AltName: Full=Absent in melanoma 1 protein {ECO:0000303|PubMed:9096375};
GN Name=CRYBG1 {ECO:0000312|HGNC:HGNC:356};
GN Synonyms=AIM1 {ECO:0000303|PubMed:9096375};
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 [GENOMIC DNA] OF 1-86 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 87-1723, AND VARIANTS PRO-293; ALA-1196 AND TYR-1395.
RC TISSUE=Liver;
RX PubMed=9096375; DOI=10.1073/pnas.94.7.3229;
RA Ray M.E., Wistow G., Su Y.A., Meltzer P.S., Trent J.M.;
RT "AIM1, a novel non-lens member of the betagamma-crystallin superfamily, is
RT associated with the control of tumorigenicity in human malignant
RT melanoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3229-3234(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-329 AND THR-525, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-81 AND SER-348, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP STRUCTURE BY NMR OF 1416-1495.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fifth crystallin domain of the non-lens protein,
RT absent in melanoma 1.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 1022-1117.
RX PubMed=18582473; DOI=10.1016/j.jmb.2008.06.019;
RA Aravind P., Wistow G., Sharma Y., Sankaranarayanan R.;
RT "Exploring the limits of sequence and structure in a variant betagamma-
RT crystallin domain of the protein absent in melanoma-1 (AIM1).";
RL J. Mol. Biol. 381:509-518(2008).
CC -!- FUNCTION: May function as suppressor of malignant melanoma. It may
CC exert its effects through interactions with the cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4K1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4K1-2; Sequence=VSP_056580, VSP_056581;
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; U83116; AAB53792.1; -; Genomic_DNA.
DR EMBL; U83115; AAB53791.1; -; mRNA.
DR EMBL; AK300443; BAG62166.1; -; mRNA.
DR EMBL; AL359292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48412.1; -; Genomic_DNA.
DR CCDS; CCDS34506.1; -. [Q9Y4K1-1]
DR RefSeq; NP_001615.2; NM_001624.3. [Q9Y4K1-1]
DR PDB; 2DAD; NMR; -; A=1416-1495.
DR PDB; 3CW3; X-ray; 1.88 A; A=1022-1117.
DR PDB; 6VRO; X-ray; 2.45 A; B=716-741.
DR PDBsum; 2DAD; -.
DR PDBsum; 3CW3; -.
DR PDBsum; 6VRO; -.
DR AlphaFoldDB; Q9Y4K1; -.
DR SMR; Q9Y4K1; -.
DR BioGRID; 106705; 101.
DR ELM; Q9Y4K1; -.
DR IntAct; Q9Y4K1; 18.
DR MINT; Q9Y4K1; -.
DR STRING; 9606.ENSP00000358062; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR GlyConnect; 2023; 2 N-Linked glycans (1 site).
DR GlyGen; Q9Y4K1; 3 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; Q9Y4K1; -.
DR PhosphoSitePlus; Q9Y4K1; -.
DR SwissPalm; Q9Y4K1; -.
DR BioMuta; CRYBG1; -.
DR DMDM; 76800646; -.
DR EPD; Q9Y4K1; -.
DR jPOST; Q9Y4K1; -.
DR MassIVE; Q9Y4K1; -.
DR MaxQB; Q9Y4K1; -.
DR PaxDb; Q9Y4K1; -.
DR PeptideAtlas; Q9Y4K1; -.
DR PRIDE; Q9Y4K1; -.
DR ProteomicsDB; 5139; -.
DR ProteomicsDB; 86224; -. [Q9Y4K1-1]
DR DNASU; 202; -.
DR GeneID; 202; -.
DR KEGG; hsa:202; -.
DR UCSC; uc003prh.4; human. [Q9Y4K1-1]
DR CTD; 202; -.
DR DisGeNET; 202; -.
DR GeneCards; CRYBG1; -.
DR HGNC; HGNC:356; CRYBG1.
DR MIM; 601797; gene.
DR neXtProt; NX_Q9Y4K1; -.
DR PharmGKB; PA24649; -.
DR eggNOG; ENOG502QUA4; Eukaryota.
DR HOGENOM; CLU_002648_0_0_1; -.
DR InParanoid; Q9Y4K1; -.
DR PhylomeDB; Q9Y4K1; -.
DR TreeFam; TF331078; -.
DR PathwayCommons; Q9Y4K1; -.
DR SignaLink; Q9Y4K1; -.
DR BioGRID-ORCS; 202; 8 hits in 1054 CRISPR screens.
DR ChiTaRS; AIM1; human.
DR EvolutionaryTrace; Q9Y4K1; -.
DR GeneWiki; AIM1; -.
DR GenomeRNAi; 202; -.
DR Pharos; Q9Y4K1; Tbio.
DR PRO; PR:Q9Y4K1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y4K1; protein.
DR Genevisible; Q9Y4K1; HS.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR011024; G_crystallin-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00030; Crystall; 6.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR01367; BGCRYSTALLIN.
DR SMART; SM00458; RICIN; 1.
DR SMART; SM00247; XTALbg; 6.
DR SUPFAM; SSF49695; SSF49695; 3.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 12.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lectin; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1723
FT /note="Beta/gamma crystallin domain-containing protein 1"
FT /id="PRO_0000057609"
FT DOMAIN 1022..1061
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1062..1117
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1123..1163
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1164..1206
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1218..1270
FT /note="Beta/gamma crystallin 'Greek key' 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1271..1313
FT /note="Beta/gamma crystallin 'Greek key' 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1319..1361
FT /note="Beta/gamma crystallin 'Greek key' 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1362..1404
FT /note="Beta/gamma crystallin 'Greek key' 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1415..1452
FT /note="Beta/gamma crystallin 'Greek key' 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1453..1496
FT /note="Beta/gamma crystallin 'Greek key' 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1502..1542
FT /note="Beta/gamma crystallin 'Greek key' 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1543..1584
FT /note="Beta/gamma crystallin 'Greek key' 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 1586..1719
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 1..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 525
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..26
FT /note="MEKRSSGRRSGRRRGSQKSTDSPGAD -> MQKPKTVAWENLGPEMSALGTA
FT FSRE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056580"
FT VAR_SEQ 27..1207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056581"
FT VARIANT 267
FT /note="G -> D (in dbSNP:rs11968933)"
FT /id="VAR_055687"
FT VARIANT 293
FT /note="Q -> P (in dbSNP:rs1159148)"
FT /evidence="ECO:0000269|PubMed:9096375"
FT /id="VAR_055688"
FT VARIANT 491
FT /note="C -> R (in dbSNP:rs3747787)"
FT /id="VAR_055689"
FT VARIANT 1096
FT /note="L -> V (in dbSNP:rs1350902)"
FT /id="VAR_055690"
FT VARIANT 1196
FT /note="E -> A (in dbSNP:rs783396)"
FT /evidence="ECO:0000269|PubMed:9096375"
FT /id="VAR_055691"
FT VARIANT 1395
FT /note="C -> Y (in dbSNP:rs2297970)"
FT /evidence="ECO:0000269|PubMed:9096375"
FT /id="VAR_055692"
FT VARIANT 1445
FT /note="T -> S (in dbSNP:rs1676015)"
FT /id="VAR_055693"
FT STRAND 1023..1028
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1037..1039
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1053..1069
FT /evidence="ECO:0007829|PDB:3CW3"
FT TURN 1070..1072
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1073..1079
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1081..1088
FT /evidence="ECO:0007829|PDB:3CW3"
FT HELIX 1094..1096
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1098..1100
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1112..1116
FT /evidence="ECO:0007829|PDB:3CW3"
FT STRAND 1416..1422
FT /evidence="ECO:0007829|PDB:2DAD"
FT TURN 1423..1425
FT /evidence="ECO:0007829|PDB:2DAD"
FT STRAND 1426..1434
FT /evidence="ECO:0007829|PDB:2DAD"
FT HELIX 1440..1442
FT /evidence="ECO:0007829|PDB:2DAD"
FT STRAND 1446..1460
FT /evidence="ECO:0007829|PDB:2DAD"
FT STRAND 1472..1477
FT /evidence="ECO:0007829|PDB:2DAD"
FT HELIX 1478..1481
FT /evidence="ECO:0007829|PDB:2DAD"
FT STRAND 1491..1495
FT /evidence="ECO:0007829|PDB:2DAD"
SQ SEQUENCE 1723 AA; 188676 MW; F4137765BCE039D5 CRC64;
MEKRSSGRRS GRRRGSQKST DSPGADAELP ESAARDDAVF DDEVAPNAAS DNASAEKKVK
SPRAALDGGV ASAASPESKP SPGTKGQLRG ESDRSKQPPP ASSPTKRKGR SRALEAVPAP
PASGPRAPAK ESPPKRVPDP SPVTKGTAAE SGEEAARAIP RELPVKSSSL LPEIKPEHKR
GPLPNHFNGR AEGGRSRELG RAAGAPGASD ADGLKPRNHF GVGRSTVTTK VTLPAKPKHV
ELNLKTPKNL DSLGNEHNPF SQPVHKGNTA TKISLFENKR TNSSPRHTDI RGQRNTPASS
KTFVGRAKLN LAKKAKEMEQ PEKKVMPNSP QNGVLVKETA IETKVTVSEE EILPATRGMN
GDSSENQALG PQPNQDDKAD VQTDAGCLSE PVASALIPVK DHKLLEKEDS EAADSKSLVL
ENVTDTAQDI PTTVDTKDLP PTAMPKPQHT FSDSQSPAES SPGPSLSLSA PAPGDVPKDT
CVQSPISSFP CTDLKVSENH KGCVLPVSRQ NNEKMPLLEL GGETTPPLST ERSPEAVGSE
CPSRVLVQVR SFVLPVESTQ DVSSQVIPES SEVREVQLPT CHSNEPEVVS VASCAPPQEE
VLGNEHSHCT AELAAKSGPQ VIPPASEKTL PIQAQSQGSR TPLMAESSPT NSPSSGNHLA
TPQRPDQTVT NGQDSPASLL NISAGSDDSV FDSSSDMEKF TEIIKQMDSA VCMPMKRKKA
RMPNSPAPHF AMPPIHEDHL EKVFDPKVFT FGLGKKKESQ PEMSPALHLM QNLDTKSKLR
PKRASAEQSV LFKSLHTNTN GNSEPLVMPE INDKENRDVT NGGIKRSRLE KSALFSSLLS
SLPQDKIFSP SVTSVNTMTT AFSTSQNGSL SQSSVSQPTT EGAPPCGLNK EQSNLLPDNS
LKVFNFNSSS TSHSSLKSPS HMEKYPQKEK TKEDLDSRSN LHLPETKFSE LSKLKNDDME
KANHIESVIK SNLPNCANSD TDFMGLFKSS RYDPSISFSG MSLSDTMTLR GSVQNKLNPR
PGKVVIYSEP DVSEKCIEVF SDIQDCSSWS LSPVILIKVV RGCWILYEQP NFEGHSIPLE
EGELELSGLW GIEDILERHE EAESDKPVVI GSIRHVVQDY RVSHIDLFTE PEGLGILSSY
FDDTEEMQGF GVMQKTCSMK VHWGTWLIYE EPGFQGVPFI LEPGEYPDLS FWDTEEAYIG
SMRPLKMGGR KVEFPTDPKV VVYEKPFFEG KCVELETGMC SFVMEGGETE EATGDDHLPF
TSVGSMKVLR GIWVAYEKPG FTGHQYLLEE GEYRDWKAWG GYNGELQSLR PILGDFSNAH
MIMYSEKNFG SKGSSIDVLG IVANLKETGY GVKTQSINVL SGVWVAYENP DFTGEQYILD
KGFYTSFEDW GGKNCKISSV QPICLDSFTG PRRRNQIHLF SEPQFQGHSQ SFEETTSQID
DSFSTKSCRV SGGSWVVYDG ENFTGNQYVL EEGHYPCLSA MGCPPGATFK SLRFIDVEFS
EPTIILFERE DFKGKKIELN AETVNLRSLG FNTQIRSVQV IGGIWVTYEY GSYRGRQFLL
SPAEVPNWYE FSGCRQIGSL RPFVQKRIYF RLRNKATGLF MSTNGNLEDL KLLRIQVMED
VGADDQIWIY QEGCIKCRIA EDCCLTIVGS LVTSGSKLGL ALDQNADSQF WSLKSDGRIY
SKLKPNLVLD IKGGTQYDQN HIILNTVSKE KFTQVWEAMV LYT
