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TROAP_HUMAN
ID   TROAP_HUMAN             Reviewed;         778 AA.
AC   Q12815; F8VSF9; Q6PJU7; Q8N5B2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Tastin;
DE   AltName: Full=Trophinin-assisting protein;
DE   AltName: Full=Trophinin-associated protein;
GN   Name=TROAP;
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).
RX   PubMed=7758945; DOI=10.1101/gad.9.10.1199;
RA   Fukuda M.N., Sato T., Nakayama J., Klier G., Mikami M., Aoki D., Nozawa S.;
RT   "Trophinin and tastin, a novel cell adhesion molecule complex with
RT   potential involvement in embryo implantation.";
RL   Genes Dev. 9:1199-1210(1995).
RN   [2]
RP   SEQUENCE REVISION TO 714 AND 742.
RA   Fukuda M., Sato T.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
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] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Lymph;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND SER-344, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-334 AND SER-376, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-324; SER-334; SER-362
RP   AND THR-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-98; SER-170; SER-334
RP   AND SER-376, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
CC   -!- FUNCTION: Could be involved with bystin and trophinin in a cell
CC       adhesion molecule complex that mediates an initial attachment of the
CC       blastocyst to uterine epithelial cells at the time of the embryo
CC       implantation.
CC   -!- SUBUNIT: Directly binds bystin, and indirectly trophinin.
CC   -!- INTERACTION:
CC       Q12815; Q8N9N5: BANP; NbExp=3; IntAct=EBI-2349743, EBI-744695;
CC       Q12815; Q13895: BYSL; NbExp=9; IntAct=EBI-2349743, EBI-358049;
CC       Q12815; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-2349743, EBI-11976299;
CC       Q12815; Q13627: DYRK1A; NbExp=4; IntAct=EBI-2349743, EBI-1053596;
CC       Q12815; Q9Y463: DYRK1B; NbExp=7; IntAct=EBI-2349743, EBI-634187;
CC       Q12815; Q15303: ERBB4; NbExp=3; IntAct=EBI-2349743, EBI-80371;
CC       Q12815; O75420: GIGYF1; NbExp=3; IntAct=EBI-2349743, EBI-947774;
CC       Q12815; Q15323: KRT31; NbExp=3; IntAct=EBI-2349743, EBI-948001;
CC       Q12815; Q6A162: KRT40; NbExp=3; IntAct=EBI-2349743, EBI-10171697;
CC       Q12815; Q15691: MAPRE1; NbExp=9; IntAct=EBI-2349743, EBI-1004115;
CC       Q12815; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-2349743, EBI-726739;
CC       Q12815; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2349743, EBI-22310682;
CC       Q12815; O43482: OIP5; NbExp=3; IntAct=EBI-2349743, EBI-536879;
CC       Q12815; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2349743, EBI-11952721;
CC       Q12815; Q12933: TRAF2; NbExp=5; IntAct=EBI-2349743, EBI-355744;
CC       Q12815; P36406: TRIM23; NbExp=5; IntAct=EBI-2349743, EBI-740098;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q12815-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12815-2; Sequence=VSP_042820, VSP_042821;
CC       Name=3;
CC         IsoId=Q12815-3; Sequence=VSP_055063;
CC   -!- TISSUE SPECIFICITY: Strong expression at implantation sites. Was
CC       exclusively localized to the apical side of the syncytiotrophoblast.
CC       Also found in macrophages.
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DR   EMBL; U04810; AAA79333.2; -; mRNA.
DR   EMBL; AC125611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471111; EAW58064.1; -; Genomic_DNA.
DR   EMBL; BC011597; AAH11597.1; -; mRNA.
DR   EMBL; BC018627; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC032583; AAH32583.1; -; mRNA.
DR   CCDS; CCDS41779.1; -. [Q12815-2]
DR   CCDS; CCDS61117.1; -. [Q12815-3]
DR   CCDS; CCDS8784.1; -. [Q12815-1]
DR   PIR; I38487; I38487.
DR   RefSeq; NP_001094090.1; NM_001100620.1. [Q12815-2]
DR   RefSeq; NP_001265253.1; NM_001278324.1. [Q12815-3]
DR   RefSeq; NP_005471.3; NM_005480.3. [Q12815-1]
DR   RefSeq; XP_011536027.1; XM_011537725.2.
DR   AlphaFoldDB; Q12815; -.
DR   SMR; Q12815; -.
DR   BioGRID; 115341; 59.
DR   DIP; DIP-52951N; -.
DR   IntAct; Q12815; 38.
DR   MINT; Q12815; -.
DR   STRING; 9606.ENSP00000257909; -.
DR   GlyGen; Q12815; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q12815; -.
DR   PhosphoSitePlus; Q12815; -.
DR   BioMuta; TROAP; -.
DR   DMDM; 223634724; -.
DR   EPD; Q12815; -.
DR   jPOST; Q12815; -.
DR   MassIVE; Q12815; -.
DR   MaxQB; Q12815; -.
DR   PaxDb; Q12815; -.
DR   PeptideAtlas; Q12815; -.
DR   PRIDE; Q12815; -.
DR   ProteomicsDB; 28603; -.
DR   ProteomicsDB; 58966; -. [Q12815-1]
DR   ProteomicsDB; 58967; -. [Q12815-2]
DR   Antibodypedia; 25932; 79 antibodies from 20 providers.
DR   DNASU; 10024; -.
DR   Ensembl; ENST00000257909.8; ENSP00000257909.3; ENSG00000135451.13. [Q12815-1]
DR   Ensembl; ENST00000380327.9; ENSP00000369684.5; ENSG00000135451.13. [Q12815-2]
DR   Ensembl; ENST00000548311.5; ENSP00000448313.1; ENSG00000135451.13. [Q12815-3]
DR   GeneID; 10024; -.
DR   KEGG; hsa:10024; -.
DR   MANE-Select; ENST00000257909.8; ENSP00000257909.3; NM_005480.4; NP_005471.3.
DR   UCSC; uc001rtv.5; human. [Q12815-1]
DR   CTD; 10024; -.
DR   DisGeNET; 10024; -.
DR   GeneCards; TROAP; -.
DR   HGNC; HGNC:12327; TROAP.
DR   HPA; ENSG00000135451; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR   MIM; 603872; gene.
DR   neXtProt; NX_Q12815; -.
DR   OpenTargets; ENSG00000135451; -.
DR   PharmGKB; PA37003; -.
DR   VEuPathDB; HostDB:ENSG00000135451; -.
DR   eggNOG; ENOG502S991; Eukaryota.
DR   GeneTree; ENSGT00390000012132; -.
DR   HOGENOM; CLU_020167_0_0_1; -.
DR   InParanoid; Q12815; -.
DR   PhylomeDB; Q12815; -.
DR   TreeFam; TF338049; -.
DR   PathwayCommons; Q12815; -.
DR   SignaLink; Q12815; -.
DR   BioGRID-ORCS; 10024; 41 hits in 1081 CRISPR screens.
DR   ChiTaRS; TROAP; human.
DR   GeneWiki; TROAP; -.
DR   GenomeRNAi; 10024; -.
DR   Pharos; Q12815; Tbio.
DR   PRO; PR:Q12815; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q12815; protein.
DR   Bgee; ENSG00000135451; Expressed in oocyte and 137 other tissues.
DR   ExpressionAtlas; Q12815; baseline and differential.
DR   Genevisible; Q12815; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   InterPro; IPR026133; Tastin.
DR   PANTHER; PTHR15289; PTHR15289; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cytoplasm; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..778
FT                   /note="Tastin"
FT                   /id="PRO_0000065636"
FT   REPEAT          516..548
FT                   /note="1"
FT   REPEAT          549..581
FT                   /note="2"
FT   REPEAT          582..614
FT                   /note="3"
FT   REPEAT          615..647
FT                   /note="4"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..647
FT                   /note="4 X 33 AA approximate tandem repeats"
FT   REGION          600..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..529
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..631
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         363
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         113..778
FT                   /note="EAPGTIEFVADPAALATILSGEGVKSCHLGRQPSLAKRVLVRGSQGGTTQRV
FT                   QGVRASAYLAPRTPTHRLDPARASCFSRLEGPGPRGRTLCPQRLQALISPSGPSFHPST
FT                   RPSFQELRRETAGSSRTSVSQASGLLLETPVQPAFSLPKGEREVVTHSDEGGVASLGLA
FT                   QRVPLRENREMSHTRDSHDSHLMPSPAPVAQPLPGHVVPCPSPFGRAQRVPSPGPPTLT
FT                   SYSVLRRLTVQPKTRFTPMPSTPRVQQAQWLRGVSPQSCSEDPALPWEQVAVRLFDQES
FT                   CIRSLEGSGKPPVATPSGPHSNRTPSLQEVKIQRIGILQQLLRQEVEGLVGGQCVPLNG
FT                   GSSLDMVELQPLLTEISRTLNATEHNSGTSHLPGLLKHSGLPKPCLPEECGEPQPCPPA
FT                   EPGPPEAFCRSEPEIPEPSLQEQLEVPEPYPPAEPRPLESCCRSEPEIPESSRQEQLEV
FT                   PEPCPPAEPRPLESYCRIEPEIPESSRQEQLEVPEPCPPAEPGPLQPSTQGQSGPPGPC
FT                   PRVELGASEPCTLEHRSLESSLPPCCSQWAPATTSLIFSSQHPLCASPPICSLQSLRPP
FT                   AGQAGLSNLAPRTLALRERLKSCLTAIHCFHEARLDDECAFYTSRAPPSGPTRVCTNPV
FT                   ATLLEWQDALCFIPVGSAAPQGSP -> GAMACTCNHSYSGG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055063"
FT   VAR_SEQ         113..144
FT                   /note="EAPGTIEFVADPAALATILSGEGVKSCHLGRQ -> VLVPAPGKLFALRRSP
FT                   FPPAKCHLARCHGLYL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042820"
FT   VAR_SEQ         145..778
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042821"
FT   CONFLICT        224
FT                   /note="R -> H (in Ref. 1; AAA79333)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   778 AA;  83857 MW;  530B0481EC8D7E02 CRC64;
     MTTRQATKDP LLRGVSPTPS KIPVRSQKRT PFPTVTSCAV DQENQDPRRW VQKPPLNIQR
     PLVDSAGPRP KARHQAETSQ RLVGISQPRN PLEELRPSPR GQNVGPGPPA QTEAPGTIEF
     VADPAALATI LSGEGVKSCH LGRQPSLAKR VLVRGSQGGT TQRVQGVRAS AYLAPRTPTH
     RLDPARASCF SRLEGPGPRG RTLCPQRLQA LISPSGPSFH PSTRPSFQEL RRETAGSSRT
     SVSQASGLLL ETPVQPAFSL PKGEREVVTH SDEGGVASLG LAQRVPLREN REMSHTRDSH
     DSHLMPSPAP VAQPLPGHVV PCPSPFGRAQ RVPSPGPPTL TSYSVLRRLT VQPKTRFTPM
     PSTPRVQQAQ WLRGVSPQSC SEDPALPWEQ VAVRLFDQES CIRSLEGSGK PPVATPSGPH
     SNRTPSLQEV KIQRIGILQQ LLRQEVEGLV GGQCVPLNGG SSLDMVELQP LLTEISRTLN
     ATEHNSGTSH LPGLLKHSGL PKPCLPEECG EPQPCPPAEP GPPEAFCRSE PEIPEPSLQE
     QLEVPEPYPP AEPRPLESCC RSEPEIPESS RQEQLEVPEP CPPAEPRPLE SYCRIEPEIP
     ESSRQEQLEV PEPCPPAEPG PLQPSTQGQS GPPGPCPRVE LGASEPCTLE HRSLESSLPP
     CCSQWAPATT SLIFSSQHPL CASPPICSLQ SLRPPAGQAG LSNLAPRTLA LRERLKSCLT
     AIHCFHEARL DDECAFYTSR APPSGPTRVC TNPVATLLEW QDALCFIPVG SAAPQGSP
 
 
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