SGO2_HUMAN
ID SGO2_HUMAN Reviewed; 1265 AA.
AC Q562F6; Q53RR9; Q53T20; Q86XY4; Q8IWK2; Q8IZK1; Q8N1Q5; Q96LQ3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Shugoshin 2 {ECO:0000312|HGNC:HGNC:30812};
DE AltName: Full=Shugoshin-2;
DE AltName: Full=Shugoshin-like 2;
DE AltName: Full=Tripin;
GN Name=SGO2 {ECO:0000312|HGNC:HGNC:30812}; Synonyms=SGOL2;
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), AND VARIANTS VAL-496 AND SER-660.
RA Oliveira V., Fiorentino L., Chan H., Matsuzawa S., Chu Z., Saraiva M.J.,
RA Reed J.C.;
RT "Cloning and characterization of TRIPIN: an inhibitor of TRIP function on
RT TRAF2 mediated activation of NF-kB.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 698-1265 (ISOFORM 1).
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 MRNA].
RC TISSUE=Colon endothelium;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ASP-9.
RC TISSUE=Lymph, Testis, and Uterus;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP2CA.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP2CA.
RX PubMed=17485487; DOI=10.1083/jcb.200701122;
RA Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D.,
RA Muschel R., Chan G.K., Yen T.J.;
RT "Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective
RT kinetochore attachments.";
RL J. Cell Biol. 177:413-424(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1144, AND IDENTIFICATION BY
RP 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 [9]
RP INTERACTION WITH CDCA8, AND FUNCTION.
RX PubMed=20739936; DOI=10.1038/nature09390;
RA Tsukahara T., Tanno Y., Watanabe Y.;
RT "Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation.";
RL Nature 467:719-723(2010).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; PLK1 AND DYNLL1.
RX PubMed=21402792; DOI=10.1083/jcb.201008023;
RA Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.;
RT "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and
RT facilitates chromosome alignment.";
RL J. Cell Biol. 192:959-968(2011).
CC -!- FUNCTION: Cooperates with PPP2CA to protect centromeric cohesin from
CC separase-mediated cleavage in oocytes specifically during meiosis I.
CC Has a crucial role in protecting REC8 at centromeres from cleavage by
CC separase. During meiosis, protects centromeric cohesion complexes until
CC metaphase II/anaphase II transition, preventing premature release of
CC meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is
CC thus essential for an accurate gametogenesis. May act by targeting
CC PPP2CA to centromeres, thus leading to cohesin dephosphorylation (By
CC similarity). Essential for recruiting KIF2C to the inner centromere and
CC for correcting defective kinetochore attachments. Involved in
CC centromeric enrichment of AUKRB in prometaphase. {ECO:0000250,
CC ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:17485487,
CC ECO:0000269|PubMed:20739936}.
CC -!- SUBUNIT: Directly interacts with PPP2CA. Part of an astrin (SPAG5)
CC -kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and
CC SGO2. Interacts with CDCA8. {ECO:0000269|PubMed:16541025,
CC ECO:0000269|PubMed:17485487, ECO:0000269|PubMed:20739936,
CC ECO:0000269|PubMed:21402792}.
CC -!- INTERACTION:
CC Q562F6; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-989213, EBI-979174;
CC Q562F6; Q13257: MAD2L1; NbExp=10; IntAct=EBI-989213, EBI-78203;
CC Q562F6; Q15013: MAD2L1BP; NbExp=2; IntAct=EBI-989213, EBI-712181;
CC Q562F6; P62136: PPP1CA; NbExp=4; IntAct=EBI-989213, EBI-357253;
CC Q562F6-3; Q01105-2: SET; NbExp=3; IntAct=EBI-12111430, EBI-7481343;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17485487}.
CC Chromosome, centromere {ECO:0000269|PubMed:17485487}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q7TSY8}. Note=During
CC meiosis I, accumulates at centromeres during diplotene, and colocalizes
CC differentially with the cohesin subunits RAD21 and REC8 at metaphase I
CC centromeres (By similarity). SGO2 and RAD21 change their relative
CC distributions during telophase I when sister-kinetochore association is
CC lost (By similarity). During meiosis II, it shows a striking tension-
CC dependent redistribution within centromeres throughout chromosome
CC congression during prometaphase II, as it does during mitosis (By
CC similarity). In Hela cells, localizes at centromeres throughout
CC prophase until metaphase and disappears at anaphase (PubMed:17485487).
CC Centromeric localization requires the presence of BUB1 and AUKRB
CC (PubMed:17485487). {ECO:0000250|UniProtKB:Q7TSY8,
CC ECO:0000269|PubMed:17485487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q562F6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q562F6-2; Sequence=VSP_016800;
CC Name=3;
CC IsoId=Q562F6-3; Sequence=VSP_016798, VSP_016799;
CC -!- MISCELLANEOUS: Shugoshin is Japanese for guardian spirit (as it is
CC known to be a protector of centromeric cohesin).
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35764.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB71617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04524.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY094614; AAM21971.1; -; mRNA.
DR EMBL; AK057940; BAB71617.1; ALT_INIT; mRNA.
DR EMBL; AK095291; BAC04524.1; ALT_FRAME; mRNA.
DR EMBL; BX647433; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC012459; AAY24310.1; -; Genomic_DNA.
DR EMBL; AC080164; AAY24264.1; -; Genomic_DNA.
DR EMBL; BC035764; AAH35764.1; ALT_SEQ; mRNA.
DR EMBL; BC048349; AAH48349.1; -; mRNA.
DR EMBL; BC092412; AAH92412.1; -; mRNA.
DR CCDS; CCDS42796.1; -. [Q562F6-1]
DR RefSeq; NP_001153518.1; NM_001160046.1. [Q562F6-2]
DR RefSeq; NP_689737.4; NM_152524.5. [Q562F6-1]
DR RefSeq; XP_005246402.1; XM_005246345.3. [Q562F6-1]
DR RefSeq; XP_011509036.1; XM_011510734.2. [Q562F6-1]
DR AlphaFoldDB; Q562F6; -.
DR SMR; Q562F6; -.
DR BioGRID; 127357; 64.
DR CORUM; Q562F6; -.
DR DIP; DIP-36615N; -.
DR IntAct; Q562F6; 45.
DR MINT; Q562F6; -.
DR STRING; 9606.ENSP00000350447; -.
DR iPTMnet; Q562F6; -.
DR PhosphoSitePlus; Q562F6; -.
DR BioMuta; SGO2; -.
DR DMDM; 85542144; -.
DR CPTAC; CPTAC-946; -.
DR EPD; Q562F6; -.
DR jPOST; Q562F6; -.
DR MassIVE; Q562F6; -.
DR MaxQB; Q562F6; -.
DR PaxDb; Q562F6; -.
DR PeptideAtlas; Q562F6; -.
DR PRIDE; Q562F6; -.
DR ProteomicsDB; 62559; -. [Q562F6-1]
DR ProteomicsDB; 62560; -. [Q562F6-2]
DR ProteomicsDB; 62561; -. [Q562F6-3]
DR Antibodypedia; 34099; 118 antibodies from 23 providers.
DR DNASU; 151246; -.
DR Ensembl; ENST00000357799.9; ENSP00000350447.4; ENSG00000163535.18. [Q562F6-1]
DR Ensembl; ENST00000409203.3; ENSP00000386249.3; ENSG00000163535.18. [Q562F6-3]
DR GeneID; 151246; -.
DR KEGG; hsa:151246; -.
DR MANE-Select; ENST00000357799.9; ENSP00000350447.4; NM_152524.6; NP_689737.4.
DR UCSC; uc002uvv.5; human. [Q562F6-1]
DR CTD; 151246; -.
DR DisGeNET; 151246; -.
DR GeneCards; SGO2; -.
DR HGNC; HGNC:30812; SGO2.
DR HPA; ENSG00000163535; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; SGO2; -.
DR MIM; 612425; gene.
DR neXtProt; NX_Q562F6; -.
DR OpenTargets; ENSG00000163535; -.
DR PharmGKB; PA134901462; -.
DR VEuPathDB; HostDB:ENSG00000163535; -.
DR eggNOG; ENOG502S9Y1; Eukaryota.
DR GeneTree; ENSGT00940000154107; -.
DR HOGENOM; CLU_264434_0_0_1; -.
DR InParanoid; Q562F6; -.
DR OMA; LNWNNEI; -.
DR OrthoDB; 290088at2759; -.
DR PhylomeDB; Q562F6; -.
DR TreeFam; TF350100; -.
DR PathwayCommons; Q562F6; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q562F6; -.
DR BioGRID-ORCS; 151246; 49 hits in 1082 CRISPR screens.
DR ChiTaRS; SGO2; human.
DR GeneWiki; SGOL2; -.
DR GenomeRNAi; 151246; -.
DR Pharos; Q562F6; Tbio.
DR PRO; PR:Q562F6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q562F6; protein.
DR Bgee; ENSG00000163535; Expressed in oocyte and 158 other tissues.
DR ExpressionAtlas; Q562F6; baseline and differential.
DR Genevisible; Q562F6; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0030892; C:mitotic cohesin complex; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR InterPro; IPR026706; SGO2.
DR InterPro; IPR038889; Shugoshin.
DR PANTHER; PTHR21577; PTHR21577; 4.
DR PANTHER; PTHR21577:SF5; PTHR21577:SF5; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Kinetochore; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1265
FT /note="Shugoshin 2"
FT /id="PRO_0000055439"
FT REGION 161..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..116
FT /evidence="ECO:0000255"
FT COILED 452..476
FT /evidence="ECO:0000255"
FT COILED 603..626
FT /evidence="ECO:0000255"
FT COMPBIAS 162..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 235..247
FT /note="ESHSHSDQSSKTS -> GEIVLKIHFEYLY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016798"
FT VAR_SEQ 248..1265
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016799"
FT VAR_SEQ 1261..1265
FT /note="DKMRR -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016800"
FT VARIANT 9
FT /note="G -> D (in dbSNP:rs1036533)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024784"
FT VARIANT 343
FT /note="E -> A (in dbSNP:rs13417812)"
FT /id="VAR_057178"
FT VARIANT 496
FT /note="I -> V (in dbSNP:rs17448235)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_024785"
FT VARIANT 660
FT /note="N -> S (in dbSNP:rs17532665)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_057179"
FT VARIANT 1099
FT /note="I -> T (in dbSNP:rs11896759)"
FT /id="VAR_057180"
FT VARIANT 1143
FT /note="H -> R (in dbSNP:rs16833776)"
FT /id="VAR_057181"
FT CONFLICT 122
FT /note="I -> T (in Ref. 3; BX647433)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="I -> V (in Ref. 3; BX647433)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="S -> R (in Ref. 1; AAM21971)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="E -> G (in Ref. 1; AAM21971)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="N -> H (in Ref. 1; AAM21971)"
FT /evidence="ECO:0000305"
FT CONFLICT 450..451
FT /note="FI -> LF (in Ref. 1; AAM21971)"
FT /evidence="ECO:0000305"
FT CONFLICT 1243
FT /note="T -> A (in Ref. 2; BAB71617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1265 AA; 144739 MW; 6A678CB3E6DF72D7 CRC64;
MECPVMETGS LFTSGIKRHL KDKRISKTTK LNVSLASKIK TKILNNSSIF KISLKHNNRA
LAQALSREKE NSRRITTEKM LLQKEVEKLN FENTFLRLKL NNLNKKLIDI EALMNNNLIT
AIEMSSLSEF HQSSFLLSAS KKKRISKQCK LMRLPFARVP LTSNDDEDED KEKMQCDNNI
KSKTLPDIPS SGSTTQPLST QDNSEVLFLK ENNQNVYGLD DSEHISSIVD VPPRESHSHS
DQSSKTSLMS EMRNAQSIGR RWEKPSPSNV TERKKRGSSW ESNNLSADTP CATVLDKQHI
SSPELNCNNE INGHTNETNT EMQRNKQDLP GLSSESAREP NAECMNQIED NDDFQLQKTV
YDADMDLTAS EVSKIVTVST GIKKKSNKKT NEHGMKTFRK VKDSSSEKKR ERSKRQFKNS
SDVDIGEKIE NRTERSDVLD GKRGAEDPGF IFNNEQLAQM NEQLAQVNEL KKMTLQTGFE
QGDRENVLCN KKEKRITNEQ EETYSLSQSS GKFHQESKFD KGQNSLTCNK SKASRQTFVI
HKLEKDNLLP NQKDKVTIYE NLDVTNEFHT ANLSTKDNGN LCDYGTHNIL DLKKYVTDIQ
PSEQNESNIN KLRKKVNRKT EIISGMNHMY EDNDKDVVHG LKKGNFFFKT QEDKEPISEN
IEVSKELQIP ALSTRDNENQ CDYRTQNVLG LQKQITNMYP VQQNESKVNK KLRQKVNRKT
EIISEVNHLD NDKSIEYTVK SHSLFLTQKD KEIIPGNLED PSEFETPALS TKDSGNLYDS
EIQNVLGVKH GHDMQPACQN DSKIGKKPRL NVCQKSEIIP ETNQIYENDN KGVHDLEKDN
FFSLTPKDKE TISENLQVTN EFQTVDLLIK DNGNLCDYDT QNILELKKYV TDRKSAEQNE
SKINKLRNKV NWKTEIISEM NQIYEDNDKD AHVQESYTKD LDFKVNKSKQ KLECQDIINK
HYMEVNSNEK ESCDQILDSY KVVKKRKKES SCKAKNILTK AKNKLASQLT ESSQTSISLE
SDLKHITSEA DSDPGNPVEL CKTQKQSTTT LNKKDLPFVE EIKEGECQVK KVNKMTSKSK
KRKTSIDPSP ESHEVMERIL DSVQGKSTVS EQADKENNLE NEKMVKNKPD FYTKAFRSLS
EIHSPNIQDS SFDSVREGLV PLSVSSGKNV IIKENFALEC SPAFQVSDDE HEKMNKMKFK
VNRRTQKSGI GDRPLQDLSN TSFVSNNTAE SENKSEDLSS ERTSRRRRCT PFYFKEPSLR
DKMRR
