CIRBP_HUMAN
ID CIRBP_HUMAN Reviewed; 172 AA.
AC Q14011; B3KT17; B4E2X2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Cold-inducible RNA-binding protein;
DE AltName: Full=A18 hnRNP;
DE AltName: Full=Glycine-rich RNA-binding protein CIRP;
GN Name=CIRBP; Synonyms=A18HNRNP, CIRP;
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=9434172; DOI=10.1016/s0378-1119(97)00530-1;
RA Nishiyama H., Higashitsuji H., Yokoi H., Itoh K., Danno S., Matsuda T.,
RA Fujita J.;
RT "Cloning and characterization of human CIRP (cold-inducible RNA-binding
RT protein) cDNA and chromosomal assignment of the gene.";
RL Gene 204:115-120(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9334257; DOI=10.1074/jbc.272.42.26720;
RA Sheikh M.S., Carrier F., Papathanasiou M.A., Hollander M.C., Zhan Q.,
RA Yu K., Fornace A.J. Jr.;
RT "Identification of several human homologs of hamster DNA damage-inducible
RT transcripts. Cloning and characterization of a novel UV-inducible cDNA that
RT codes for a putative RNA-binding protein.";
RL J. Biol. Chem. 272:26720-26726(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Placenta;
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, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11574538; DOI=10.1074/jbc.m105396200;
RA Yang C., Carrier F.;
RT "The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a protective
RT role in the genotoxic stress response.";
RL J. Biol. Chem. 276:47277-47284(2001).
RN [7]
RP INDUCTION BY HYPOXIA.
RX PubMed=15075239; DOI=10.1242/jcs.01026;
RA Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R., Koehne P.,
RA Fujita J., Seeger K.;
RT "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a
RT HIF-1-independent mechanism.";
RL J. Cell Sci. 117:1785-1794(2004).
RN [8]
RP FUNCTION, PHOSPHORYLATION, RNA-BINDING, INTERACTION WITH EIF4G1, AND
RP ASSOCIATION WITH RIBOSOMES.
RX PubMed=16513844; DOI=10.1093/nar/gkj519;
RA Yang R., Weber D.J., Carrier F.;
RT "Post-transcriptional regulation of thioredoxin by the stress inducible
RT heterogeneous ribonucleoprotein A18.";
RL Nucleic Acids Res. 34:1224-1236(2006).
RN [9]
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 [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-138; SER-146;
RP SER-156; SER-159 AND SER-163, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
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 [14]
RP STRUCTURE BY NMR OF 1-90.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in A18 HNRNP.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Cold-inducible mRNA binding protein that plays a protective
CC role in the genotoxic stress response by stabilizing transcripts of
CC genes involved in cell survival. Acts as a translational activator.
CC Seems to play an essential role in cold-induced suppression of cell
CC proliferation. Binds specifically to the 3'-untranslated regions (3'-
CC UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a
CC translational repressor (By similarity). Promotes assembly of stress
CC granules (SGs), when overexpressed. {ECO:0000250,
CC ECO:0000269|PubMed:11574538, ECO:0000269|PubMed:16513844}.
CC -!- SUBUNIT: Interacts with EIF4G1. Associates with ribosomes.
CC {ECO:0000269|PubMed:16513844}.
CC -!- INTERACTION:
CC Q14011; P54253: ATXN1; NbExp=7; IntAct=EBI-538850, EBI-930964;
CC Q14011; P61978: HNRNPK; NbExp=9; IntAct=EBI-538850, EBI-304185;
CC Q14011; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-538850, EBI-7060731;
CC Q14011; Q5VWX1: KHDRBS2; NbExp=4; IntAct=EBI-538850, EBI-742808;
CC Q14011; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-538850, EBI-739832;
CC Q14011; P38159: RBMX; NbExp=4; IntAct=EBI-538850, EBI-743526;
CC Q14011; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-538850, EBI-8638511;
CC Q14011; Q15415: RBMY1J; NbExp=3; IntAct=EBI-538850, EBI-8642021;
CC Q14011; P09012: SNRPA; NbExp=4; IntAct=EBI-538850, EBI-607085;
CC Q14011; P84103: SRSF3; NbExp=3; IntAct=EBI-538850, EBI-372557;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11574538}. Cytoplasm {ECO:0000269|PubMed:11574538}.
CC Note=Translocates from the nucleus to the cytoplasm after exposure to
CC UV radiation. Translocates from the nucleus to the cytoplasm into
CC stress granules upon various cytoplasmic stresses, such as osmotic and
CC heat shocks. Its recruitment into stress granules occurs in the absence
CC of TIAR proteins (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14011-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14011-2; Sequence=VSP_056402, VSP_056403;
CC Name=3;
CC IsoId=Q14011-3; Sequence=VSP_056895, VSP_056403;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: By cold stress in response to DNA damage induced by UV
CC irradiation or UV mimetic agents. Up-regulated by hypoxia.
CC {ECO:0000269|PubMed:15075239}.
CC -!- DOMAIN: Both the RRM domain and the arginine, glycine (RGG) rich domain
CC are necessary for binding to the TXN 3'-untranslated region. Both the
CC RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats)
CC are necessary for optimal recruitment into SGs upon cellular stress.
CC The C-terminal domain containing RGG repeats is necessary for
CC translational repression (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated on arginine residues. Methylation of the RGG motifs is
CC a prerequisite for recruitment into SGs (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by GSK3B
CC increases RNA-binding activity to the TXN 3'-UTR transcript upon
CC exposure to UV radiation. {ECO:0000269|PubMed:16513844}.
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DR EMBL; D78134; BAA11212.1; -; mRNA.
DR EMBL; AF021336; AAC51787.1; -; mRNA.
DR EMBL; AK094781; BAG52929.1; -; mRNA.
DR EMBL; AK304470; BAG65284.1; -; mRNA.
DR EMBL; AC004221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004258; AAC04895.1; -; Genomic_DNA.
DR EMBL; BC000403; AAH00403.1; -; mRNA.
DR EMBL; BC000901; AAH00901.1; -; mRNA.
DR CCDS; CCDS12059.1; -. [Q14011-1]
DR RefSeq; NP_001271.1; NM_001280.2. [Q14011-1]
DR RefSeq; NP_001287744.1; NM_001300815.1.
DR RefSeq; NP_001287758.1; NM_001300829.1.
DR RefSeq; XP_006722700.1; XM_006722637.1. [Q14011-1]
DR PDB; 1X5S; NMR; -; A=1-89.
DR PDB; 5TBX; X-ray; 1.77 A; A/B=1-91.
DR PDBsum; 1X5S; -.
DR PDBsum; 5TBX; -.
DR AlphaFoldDB; Q14011; -.
DR SMR; Q14011; -.
DR BioGRID; 107573; 143.
DR CORUM; Q14011; -.
DR IntAct; Q14011; 81.
DR MINT; Q14011; -.
DR STRING; 9606.ENSP00000466897; -.
DR GlyGen; Q14011; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14011; -.
DR PhosphoSitePlus; Q14011; -.
DR BioMuta; CIRBP; -.
DR DMDM; 5921786; -.
DR REPRODUCTION-2DPAGE; IPI00180954; -.
DR EPD; Q14011; -.
DR jPOST; Q14011; -.
DR MassIVE; Q14011; -.
DR MaxQB; Q14011; -.
DR PaxDb; Q14011; -.
DR PeptideAtlas; Q14011; -.
DR PRIDE; Q14011; -.
DR ProteomicsDB; 3661; -.
DR ProteomicsDB; 5861; -.
DR ProteomicsDB; 59794; -. [Q14011-1]
DR Antibodypedia; 22628; 362 antibodies from 37 providers.
DR DNASU; 1153; -.
DR Ensembl; ENST00000320936.9; ENSP00000322887.4; ENSG00000099622.14. [Q14011-1]
DR Ensembl; ENST00000413636.6; ENSP00000412831.2; ENSG00000099622.14. [Q14011-2]
DR Ensembl; ENST00000585630.5; ENSP00000466110.1; ENSG00000099622.14. [Q14011-1]
DR Ensembl; ENST00000586472.5; ENSP00000465779.1; ENSG00000099622.14. [Q14011-1]
DR Ensembl; ENST00000588030.5; ENSP00000468788.1; ENSG00000099622.14. [Q14011-1]
DR Ensembl; ENST00000588090.5; ENSP00000466207.1; ENSG00000099622.14. [Q14011-1]
DR GeneID; 1153; -.
DR KEGG; hsa:1153; -.
DR UCSC; uc010xgl.2; human. [Q14011-1]
DR CTD; 1153; -.
DR DisGeNET; 1153; -.
DR GeneCards; CIRBP; -.
DR HGNC; HGNC:1982; CIRBP.
DR HPA; ENSG00000099622; Low tissue specificity.
DR MIM; 602649; gene.
DR neXtProt; NX_Q14011; -.
DR OpenTargets; ENSG00000099622; -.
DR PharmGKB; PA26519; -.
DR VEuPathDB; HostDB:ENSG00000099622; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153524; -.
DR InParanoid; Q14011; -.
DR OrthoDB; 1475309at2759; -.
DR PhylomeDB; Q14011; -.
DR PathwayCommons; Q14011; -.
DR SignaLink; Q14011; -.
DR BioGRID-ORCS; 1153; 20 hits in 1077 CRISPR screens.
DR ChiTaRS; CIRBP; human.
DR EvolutionaryTrace; Q14011; -.
DR GeneWiki; CIRBP; -.
DR GenomeRNAi; 1153; -.
DR Pharos; Q14011; Tbio.
DR PRO; PR:Q14011; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q14011; protein.
DR Bgee; ENSG00000099622; Expressed in tibia and 199 other tissues.
DR ExpressionAtlas; Q14011; baseline and differential.
DR Genevisible; Q14011; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; TAS:ProtInc.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR CDD; cd12449; RRM_CIRBP_RBM3; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034278; RBM3/CIRBP_RRM.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Stress response.
FT CHAIN 1..172
FT /note="Cold-inducible RNA-binding protein"
FT /id="PRO_0000081503"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 69..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..69
FT /note="MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFV
FT TFENIDDAKDAMMAMNG -> MSSRWSRSSQSTDRSL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056895"
FT VAR_SEQ 83..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056402"
FT VAR_SEQ 167
FT /note="Y -> YGKSHSEGATLLWPAVGARFTLVPSPSTLGWTLRPCHCACPEEAHLS
FT SQSHFYRRTQKPNETDQKGKGERGPAGQSARCMCGRRPASLGCGGWLLPGRRPRPGLAS
FT GVKLPLVASVPLHCACFLSS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056403"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5TBX"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:5TBX"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5TBX"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:5TBX"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:5TBX"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:5TBX"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:5TBX"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5TBX"
SQ SEQUENCE 172 AA; 18648 MW; 003FABF28F5405D0 CRC64;
MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA
KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRGR GRGFSRGGGD
RGYGGNRFES RSGGYGGSRD YYSSRSQSGG YSDRSSGGSY RDSYDSYATH NE
