CR3L4_HUMAN
ID CR3L4_HUMAN Reviewed; 395 AA.
AC Q8TEY5; D3DV62; Q5T4L0; Q86YW6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 4;
DE Short=cAMP-responsive element-binding protein 3-like protein 4;
DE AltName: Full=Androgen-induced basic leucine zipper protein;
DE Short=AIbZIP;
DE AltName: Full=Attaching to CRE-like 1;
DE Short=ATCE1;
DE AltName: Full=Cyclic AMP-responsive element-binding protein 4;
DE Short=CREB-4;
DE Short=cAMP-responsive element-binding protein 4;
DE AltName: Full=Transcript induced in spermiogenesis protein 40;
DE Short=Tisp40;
DE AltName: Full=hJAL;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 4;
GN Name=CREB3L4; Synonyms=AIBZIP, CREB4, JAL;
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 TISSUE SPECIFICITY.
RX PubMed=11830526;
RA Qi H., Fillion C., Labrie Y., Grenier J., Fournier A., Berger L.,
RA El-Alfy M., Labrie C.;
RT "AIbZIP, a novel bZIP gene located on chromosome 1q21.3 that is highly
RT expressed in prostate tumors and of which the expression is up-regulated by
RT androgens in LNCaP human prostate cancer cells.";
RL Cancer Res. 62:721-733(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12111373; DOI=10.1007/s100380200053;
RA Cao G., Ni X., Jiang M., Ma Y., Cheng H., Guo L., Ji C., Gu S., Xie Y.,
RA Mao Y.;
RT "Molecular cloning and characterization of a novel human cAMP response
RT element-binding (CREB) gene (CREB4).";
RL J. Hum. Genet. 47:373-376(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Fujita K., Hatakeyama S., Ishikawa F.;
RT "Homo sapiens and Mus musculus JAL gene.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Guo J.H., Dai F.Y., Yu L.;
RT "Human ATCE1 - a novel protein that contains a CRE binding domain.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=15938716; DOI=10.1111/j.1365-2443.2005.00860.x;
RA Nagamori I., Yabuta N., Fujii T., Tanaka H., Yomogida K., Nishimune Y.,
RA Nojima H.;
RT "Tisp40, a spermatid specific bZip transcription factor, functions by
RT binding to the unfolded protein response element via the Rip pathway.";
RL Genes Cells 10:575-594(2005).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-335.
RX PubMed=16236796; DOI=10.1091/mbc.e05-06-0500;
RA Stirling J., O'hare P.;
RT "CREB4, a transmembrane bZip transcription factor and potential new
RT substrate for regulation and cleavage by S1P.";
RL Mol. Biol. Cell 17:413-426(2006).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=17270658; DOI=10.1016/j.urology.2006.11.001;
RA Levesque M.H., El-Alfy M., Berger L., Labrie F., Labrie C.;
RT "Evaluation of AIbZIP and Cdc47 as markers for human prostatic diseases.";
RL Urology 69:196-201(2007).
CC -!- FUNCTION: Transcriptional activator that may play a role in the
CC unfolded protein response. Binds to the UPR element (UPRE) but not to
CC CRE element. Preferentially binds DNA with to the consensus sequence
CC 5'-T[GT]ACGT[GA][GT]-3' and has transcriptional activation activity
CC from UPRE. Binds to NF-kappa-B site and has transcriptional activation
CC activity from NF-kappa-B-containing regulatory elements (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16236796}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8TEY5; O43681: GET3; NbExp=3; IntAct=EBI-3925424, EBI-2515857;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}. Note=May also be located
CC in Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 4]: Nucleus. Note=Under ER stress the cleaved N-
CC terminal cytoplasmic domain translocates into the nucleus.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TEY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEY5-2; Sequence=VSP_045426;
CC -!- TISSUE SPECIFICITY: According to PubMed:11830526, exclusively expressed
CC in the prostate. Expressed in breast and prostate cancer cell lines.
CC Expressed in prostatic luminal epithelial cells (at protein level).
CC Expression is significantly more abundant in prostate cancer than in
CC benign prostatic tissue (prostatic hyperplasia). According to
CC PubMed:12111373, also expressed in brain, pancreas and skeletal muscle,
CC and at lower levels in small intestine, testis, leukocyte and thymus.
CC {ECO:0000269|PubMed:11830526, ECO:0000269|PubMed:12111373,
CC ECO:0000269|PubMed:17270658}.
CC -!- INDUCTION: By androgens.
CC -!- PTM: N-glycosylated in the C-terminal region.
CC {ECO:0000269|PubMed:15938716}.
CC -!- PTM: Controlled by regulated intramembrane proteolysis (RIP). Following
CC ER stress a fragment containing the cytoplasmic transcription factor
CC domain is released by proteolysis. The cleavage seems to be performed
CC sequentially by site-1 and site-2 proteases (PS1 and PS2). PS1 cleavage
CC may be suppressed by a determinant in the C-terminal region (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; AF394167; AAL76113.1; -; mRNA.
DR EMBL; AF468007; AAO33070.1; -; mRNA.
DR EMBL; AB052778; BAC45035.1; -; mRNA.
DR EMBL; AB052781; BAC45224.1; -; Genomic_DNA.
DR EMBL; AY049977; AAL13157.1; -; mRNA.
DR EMBL; AK304665; BAG65440.1; -; mRNA.
DR EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53251.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53253.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53254.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53256.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53257.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53258.1; -; Genomic_DNA.
DR EMBL; BC038962; AAH38962.1; -; mRNA.
DR CCDS; CCDS1056.1; -. [Q8TEY5-1]
DR CCDS; CCDS58029.1; -. [Q8TEY5-2]
DR RefSeq; NP_001242907.1; NM_001255978.1. [Q8TEY5-1]
DR RefSeq; NP_001242908.1; NM_001255979.1. [Q8TEY5-1]
DR RefSeq; NP_001242909.1; NM_001255980.1. [Q8TEY5-2]
DR RefSeq; NP_001242910.1; NM_001255981.1. [Q8TEY5-2]
DR RefSeq; NP_570968.1; NM_130898.3. [Q8TEY5-1]
DR RefSeq; XP_006711235.1; XM_006711172.2. [Q8TEY5-2]
DR RefSeq; XP_016855861.1; XM_017000372.1. [Q8TEY5-2]
DR AlphaFoldDB; Q8TEY5; -.
DR SMR; Q8TEY5; -.
DR BioGRID; 127142; 13.
DR IntAct; Q8TEY5; 6.
DR STRING; 9606.ENSP00000357596; -.
DR GlyGen; Q8TEY5; 1 site.
DR iPTMnet; Q8TEY5; -.
DR PhosphoSitePlus; Q8TEY5; -.
DR BioMuta; CREB3L4; -.
DR DMDM; 74751463; -.
DR jPOST; Q8TEY5; -.
DR MassIVE; Q8TEY5; -.
DR MaxQB; Q8TEY5; -.
DR PaxDb; Q8TEY5; -.
DR PeptideAtlas; Q8TEY5; -.
DR PRIDE; Q8TEY5; -.
DR ProteomicsDB; 64469; -.
DR ProteomicsDB; 74525; -. [Q8TEY5-1]
DR Antibodypedia; 34142; 262 antibodies from 35 providers.
DR DNASU; 148327; -.
DR Ensembl; ENST00000271889.8; ENSP00000271889.4; ENSG00000143578.16. [Q8TEY5-1]
DR Ensembl; ENST00000368600.7; ENSP00000357589.3; ENSG00000143578.16. [Q8TEY5-2]
DR Ensembl; ENST00000368603.5; ENSP00000357592.1; ENSG00000143578.16. [Q8TEY5-1]
DR Ensembl; ENST00000368607.8; ENSP00000357596.3; ENSG00000143578.16. [Q8TEY5-1]
DR GeneID; 148327; -.
DR KEGG; hsa:148327; -.
DR MANE-Select; ENST00000368607.8; ENSP00000357596.3; NM_001255978.2; NP_001242907.1.
DR UCSC; uc001fdm.3; human. [Q8TEY5-1]
DR CTD; 148327; -.
DR DisGeNET; 148327; -.
DR GeneCards; CREB3L4; -.
DR HGNC; HGNC:18854; CREB3L4.
DR HPA; ENSG00000143578; Tissue enhanced (prostate).
DR MIM; 607138; gene.
DR neXtProt; NX_Q8TEY5; -.
DR OpenTargets; ENSG00000143578; -.
DR PharmGKB; PA134922919; -.
DR VEuPathDB; HostDB:ENSG00000143578; -.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000160806; -.
DR HOGENOM; CLU_047257_3_0_1; -.
DR InParanoid; Q8TEY5; -.
DR OMA; FSPFSRH; -.
DR OrthoDB; 644485at2759; -.
DR PhylomeDB; Q8TEY5; -.
DR TreeFam; TF316079; -.
DR PathwayCommons; Q8TEY5; -.
DR Reactome; R-HSA-8874211; CREB3 factors activate genes.
DR SignaLink; Q8TEY5; -.
DR BioGRID-ORCS; 148327; 20 hits in 1099 CRISPR screens.
DR ChiTaRS; CREB3L4; human.
DR GenomeRNAi; 148327; -.
DR Pharos; Q8TEY5; Tbio.
DR PRO; PR:Q8TEY5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8TEY5; protein.
DR Bgee; ENSG00000143578; Expressed in parotid gland and 146 other tissues.
DR ExpressionAtlas; Q8TEY5; baseline and differential.
DR Genevisible; Q8TEY5; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029807; CREB4.
DR PANTHER; PTHR45996:SF2; PTHR45996:SF2; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Membrane; Nucleus; Reference proteome;
KW Signal-anchor; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Unfolded protein response.
FT CHAIN 1..395
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 4"
FT /id="PRO_0000288079"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 4"
FT /id="PRO_0000296219"
FT TOPO_DOM 1..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 217..280
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 82..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..248
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 259..280
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 355..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 338..339
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 39..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045426"
FT VARIANT 95
FT /note="P -> S (in dbSNP:rs11264743)"
FT /id="VAR_048444"
FT MUTAGEN 335
FT /note="R->G: Abolishes cleavage by SP1."
FT /evidence="ECO:0000269|PubMed:16236796"
FT CONFLICT 35
FT /note="P -> L (in Ref. 2; AAO33070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 43432 MW; F3DDF288421AE5F2 CRC64;
MDLGIPDLLD AWLEPPEDIF STGSVLELGL HCPPPEVPVT RLQEQGLQGW KSGGDRGCGL
QESEPEDFLK LFIDPNEVYC SEASPGSDSG ISEDPCHPDS PPAPRATSSP MLYEVVYEAG
ALERMQGETG PNVGLISIQL DQWSPAFMVP DSCMVSELPF DAHAHILPRA GTVAPVPCTT
LLPCQTLFLT DEEKRLLGQE GVSLPSHLPL TKAEERVLKK VRRKIRNKQS AQDSRRRKKE
YIDGLESRVA ACSAQNQELQ KKVQELERHN ISLVAQLRQL QTLIAQTSNK AAQTSTCVLI
LLFSLALIIL PSFSPFQSRP EAGSEDYQPH GVTSRNILTH KDVTENLETQ VVESRLREPP
GAKDANGSTR TLLEKMGGKP RPSGRIRSVL HADEM
