RIPR1_HUMAN
ID RIPR1_HUMAN Reviewed; 1223 AA.
AC Q6ZS17; B4DEQ9; B4DIM2; E9PBS3; Q4G0A4; Q7Z5R7; Q8NDA4; Q96J39; Q96PV8;
AC Q9H8D9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Rho family-interacting cell polarization regulator 1;
GN Name=RIPOR1; Synonyms=FAM65A, KIAA1930;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Cerebellum, Hippocampus, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-1223 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-1223 (ISOFORM 1).
RC TISSUE=Cervix, Colon, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 276-1223 (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
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-349; SER-351 AND THR-355, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [10]
RP IDENTIFICATION BY 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 FUNCTION, INTERACTION WITH PDCD10; RHOA; RHOB; RHOC; STK24; STK26 AND
RP 14-3-3 PROTEINS, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=27807006; DOI=10.1242/jcs.198614;
RA Mardakheh F.K., Self A., Marshall C.J.;
RT "RHO binding to FAM65A regulates Golgi reorientation during cell
RT migration.";
RL J. Cell Sci. 129:4466-4479(2016).
CC -!- FUNCTION: Downstream effector protein for Rho-type small GTPases that
CC plays a role in cell polarity and directional migration
CC (PubMed:27807006). Acts as an adapter protein, linking active Rho
CC proteins to STK24 and STK26 kinases, and hence positively regulates
CC Golgi reorientation in polarized cell migration upon Rho activation
CC (PubMed:27807006). Involved in the subcellular relocation of STK26 from
CC the Golgi to cytoplasm punctae in a Rho- and PDCD10-dependent manner
CC upon serum stimulation (PubMed:27807006).
CC {ECO:0000269|PubMed:27807006}.
CC -!- SUBUNIT: Interacts (via N-terminus) with RHOA (GTP-bound form); this
CC interaction links active RHOA to STK24 and STK26 kinases
CC (PubMed:27807006). Interacts with RHOB (PubMed:27807006). Interacts
CC with RHOC (PubMed:27807006). Interacts (via C-terminus) with PDCD10;
CC this interaction occurs in a Rho-independent manner (PubMed:27807006).
CC Interacts (via C-terminus) with STK24; this interaction occurs in a
CC PDCD10-dependent and Rho-independent manner (PubMed:27807006).
CC Interacts (via C-terminus) with STK26; this interaction occurs in a
CC PDCD10-dependent and Rho-independent manner (PubMed:27807006).
CC Interacts (via N-terminus) with 14-3-3 proteins; these interactions
CC occur in a Rho-dependent manner (PubMed:27807006).
CC {ECO:0000269|PubMed:27807006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27807006}. Golgi
CC apparatus {ECO:0000269|PubMed:27807006}. Note=Localizes to the podocyte
CC major processes and cell body (By similarity). Colocalized with STK26
CC in the Golgi of serum-starved cells and relocated to cytoplasmic
CC punctae, probably vesicular compartments, along with STK26 upon serum
CC stimulation in a Rho- and PDCD10-dependent manner (PubMed:27807006).
CC {ECO:0000250|UniProtKB:Q68FE6, ECO:0000269|PubMed:27807006}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZS17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZS17-2; Sequence=VSP_025903;
CC Name=3;
CC IsoId=Q6ZS17-3; Sequence=VSP_043315, VSP_025903;
CC Name=4;
CC IsoId=Q6ZS17-4; Sequence=VSP_045002, VSP_025903;
CC -!- SIMILARITY: Belongs to the RIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14678.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB67823.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK023787; BAB14678.1; ALT_SEQ; mRNA.
DR EMBL; AK293748; BAG57170.1; -; mRNA.
DR EMBL; AK295677; BAG58534.1; -; mRNA.
DR EMBL; AC027682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK127792; BAC87139.1; -; mRNA.
DR EMBL; AB067517; BAB67823.1; ALT_FRAME; mRNA.
DR EMBL; BC001850; AAH01850.3; -; mRNA.
DR EMBL; BC054512; AAH54512.1; -; mRNA.
DR EMBL; BC098587; AAH98587.1; -; mRNA.
DR EMBL; AL834312; CAD38982.1; -; mRNA.
DR CCDS; CCDS10840.1; -. [Q6ZS17-2]
DR CCDS; CCDS54026.1; -. [Q6ZS17-4]
DR CCDS; CCDS54027.1; -. [Q6ZS17-3]
DR CCDS; CCDS54028.1; -. [Q6ZS17-1]
DR RefSeq; NP_001180451.1; NM_001193522.1. [Q6ZS17-1]
DR RefSeq; NP_001180452.1; NM_001193523.1. [Q6ZS17-4]
DR RefSeq; NP_001180453.1; NM_001193524.1. [Q6ZS17-3]
DR RefSeq; NP_078795.2; NM_024519.3. [Q6ZS17-2]
DR AlphaFoldDB; Q6ZS17; -.
DR SMR; Q6ZS17; -.
DR BioGRID; 122715; 15.
DR IntAct; Q6ZS17; 6.
DR MINT; Q6ZS17; -.
DR STRING; 9606.ENSP00000400099; -.
DR iPTMnet; Q6ZS17; -.
DR PhosphoSitePlus; Q6ZS17; -.
DR BioMuta; RIPOR1; -.
DR DMDM; 74711310; -.
DR EPD; Q6ZS17; -.
DR jPOST; Q6ZS17; -.
DR MassIVE; Q6ZS17; -.
DR MaxQB; Q6ZS17; -.
DR PaxDb; Q6ZS17; -.
DR PeptideAtlas; Q6ZS17; -.
DR PRIDE; Q6ZS17; -.
DR ProteomicsDB; 19285; -.
DR ProteomicsDB; 68182; -. [Q6ZS17-1]
DR ProteomicsDB; 68183; -. [Q6ZS17-2]
DR ProteomicsDB; 68184; -. [Q6ZS17-3]
DR Antibodypedia; 941; 36 antibodies from 13 providers.
DR DNASU; 79567; -.
DR Ensembl; ENST00000042381.9; ENSP00000042381.4; ENSG00000039523.20. [Q6ZS17-2]
DR Ensembl; ENST00000379312.7; ENSP00000368614.3; ENSG00000039523.20. [Q6ZS17-1]
DR Ensembl; ENST00000422602.8; ENSP00000400099.2; ENSG00000039523.20. [Q6ZS17-4]
DR Ensembl; ENST00000428437.6; ENSP00000389456.2; ENSG00000039523.20. [Q6ZS17-3]
DR GeneID; 79567; -.
DR KEGG; hsa:79567; -.
DR MANE-Select; ENST00000042381.9; ENSP00000042381.4; NM_024519.4; NP_078795.2. [Q6ZS17-2]
DR UCSC; uc002eth.4; human. [Q6ZS17-1]
DR CTD; 79567; -.
DR DisGeNET; 79567; -.
DR GeneCards; RIPOR1; -.
DR HGNC; HGNC:25836; RIPOR1.
DR HPA; ENSG00000039523; Low tissue specificity.
DR MIM; 619842; gene.
DR neXtProt; NX_Q6ZS17; -.
DR OpenTargets; ENSG00000039523; -.
DR PharmGKB; PA142671875; -.
DR VEuPathDB; HostDB:ENSG00000039523; -.
DR eggNOG; ENOG502QQ7T; Eukaryota.
DR GeneTree; ENSGT00940000153717; -.
DR HOGENOM; CLU_006211_0_0_1; -.
DR InParanoid; Q6ZS17; -.
DR OrthoDB; 1121546at2759; -.
DR PhylomeDB; Q6ZS17; -.
DR TreeFam; TF329332; -.
DR PathwayCommons; Q6ZS17; -.
DR SignaLink; Q6ZS17; -.
DR BioGRID-ORCS; 79567; 20 hits in 1079 CRISPR screens.
DR ChiTaRS; FAM65A; human.
DR GenomeRNAi; 79567; -.
DR Pharos; Q6ZS17; Tbio.
DR PRO; PR:Q6ZS17; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6ZS17; protein.
DR Bgee; ENSG00000039523; Expressed in apex of heart and 189 other tissues.
DR ExpressionAtlas; Q6ZS17; baseline and differential.
DR Genevisible; Q6ZS17; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0012506; C:vesicle membrane; TAS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
DR GO; GO:2001107; P:negative regulation of Rho guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IMP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR031780; FAM65_N.
DR InterPro; IPR026136; RIPOR3.
DR PANTHER; PTHR15829; PTHR15829; 1.
DR Pfam; PF15903; PL48; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1223
FT /note="Rho family-interacting cell polarization regulator
FT 1"
FT /id="PRO_0000289110"
FT REGION 375..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..114
FT /evidence="ECO:0000255"
FT COMPBIAS 375..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..502
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU8"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU8"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE6"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FE6"
FT VAR_SEQ 1
FT /note="M -> MNTKKRGSPARTHSM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043315"
FT VAR_SEQ 1
FT /note="M -> MTIWQMQKQAQRGSPARTHSM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045002"
FT VAR_SEQ 35..38
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11572484,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_025903"
FT CONFLICT 152
FT /note="V -> A (in Ref. 1; BAG57170)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="G -> S (in Ref. 1; BAB14678)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="A -> T (in Ref. 1; BAG57170)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="Missing (in Ref. 3; BAB67823)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="A -> T (in Ref. 1; BAB14678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1223 AA; 132308 MW; 4C6C9A387E93DEC7 CRC64;
MMSLSVRPQR RLLSARVNRS QSFAGVLGSH ERGPSLSFRS FPVFSPPGPP RKPPALSRVS
RMFSVAHPAA KVPQPERLDL VYTALKRGLT AYLEVHQQEQ EKLQGQIRES KRNSRLGFLY
DLDKQVKSIE RFLRRLEFHA SKIDELYEAY CVQRRLRDGA YNMVRAYTTG SPGSREARDS
LAEATRGHRE YTESMCLLES ELEAQLGEFH LRMKGLAGFA RLCVGDQYEI CMKYGRQRWK
LRGRIEGSGK QVWDSEETIF LPLLTEFLSI KVTELKGLAN HVVVGSVSCE TKDLFAALPQ
VVAVDINDLG TIKLSLEVTW SPFDKDDQPS AASSVNKAST VTKRFSTYSQ SPPDTPSLRE
QAFYNMLRRQ EELENGTAWS LSSESSDDSS SPQLSGTARH SPAPRPLVQQ PEPLPIQVAF
RRPETPSSGP LDEEGAVAPV LANGHAPYSR TLSHISEASV DAALAEASVE AVGPESLAWG
PSPPTHPAPT HGEHPSPVPP ALDPGHSATS STLGTTGSVP TSTDPAPSAH LDSVHKSTDS
GPSELPGPTH TTTGSTYSAI TTTHSAPSPL THTTTGSTHK PIISTLTTTG PTLNIIGPVQ
TTTSPTHTMP SPTHTTASPT HTSTSPTHTP TSPTHKTSMS PPTTTSPTPS GMGLVQTATS
PTHPTTSPTH PTTSPILINV SPSTSLELAT LSSPSKHSDP TLPGTDSLPC SPPVSNSYTQ
ADPMAPRTPH PSPAHSSRKP LTSPAPDPSE STVQSLSPTP SPPTPAPQHS DLCLAMAVQT
PVPTAAGGSG DRSLEEALGA LMAALDDYRG QFPELQGLEQ EVTRLESLLM QRQGLTRSRA
SSLSITVEHA LESFSFLNED EDEDNDVPGD RPPSSPEAGA EDSIDSPSAR PLSTGCPALD
AALVRHLYHC SRLLLKLGTF GPLRCQEAWA LERLLREARV LEAVCEFSRR WEIPASSAQE
VVQFSASRPG FLTFWDQCTE RLSCFLCPVE RVLLTFCNQY GARLSLRQPG LAEAVCVKFL
EDALGQKLPR RPQPGPGEQL TVFQFWSFVE TLDSPTMEAY VTETAEEVLL VRNLNSDDQA
VVLKALRLAP EGRLRRDGLR ALSSLLVHGN NKVMAAVSTQ LRSLSLGPTF RERALLCFLD
QLEDEDVQTR VAGCLALGCI KAPEGIEPLV YLCQTDTEAV REAARQSLQQ CGEEGQSAHR
RLEESLDALP RIFGPGSMAS TAF
