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   27-MAR-2024, entry version 168.
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.
DR   AlphaFoldDB; Q562F6; -.
DR   SMR; Q562F6; -.
DR   BioGRID; 127357; 70.
DR   CORUM; Q562F6; -.
DR   DIP; DIP-36615N; -.
DR   IntAct; Q562F6; 46.
DR   MINT; Q562F6; -.
DR   STRING; 9606.ENSP00000350447; -.
DR   GlyGen; Q562F6; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000350447; -.
DR   PeptideAtlas; Q562F6; -.
DR   ProteomicsDB; 62559; -. [Q562F6-1]
DR   ProteomicsDB; 62560; -. [Q562F6-2]
DR   ProteomicsDB; 62561; -. [Q562F6-3]
DR   Pumba; Q562F6; -.
DR   Antibodypedia; 34099; 144 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   AGR; HGNC:30812; -.
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; 5263725at2759; -.
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 1156 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 159 other cell types or tissues.
DR   ExpressionAtlas; Q562F6; baseline and differential.
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:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR   InterPro; IPR038889; Shugoshin1/2.
DR   PANTHER; PTHR21577; SHUGOSHIN; 1.
DR   PANTHER; PTHR21577:SF3; SHUGOSHIN 1-RELATED; 1.
DR   Genevisible; Q562F6; HS.
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
//