PDE1A_MOUSE
ID PDE1A_MOUSE Reviewed; 545 AA.
AC Q61481; E9Q6V1; O35388; Q5I7S8; Q8BRR9; Q9JLL9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A {ECO:0000305|PubMed:15901640};
DE Short=Cam-PDE 1A;
DE EC=3.1.4.17 {ECO:0000269|PubMed:15901640};
DE AltName: Full=61 kDa Cam-PDE;
GN Name=Pde1a {ECO:0000312|MGI:MGI:1201792};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAF63857.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, CATALYTIC ACTIVITY
RP (ISOFORM 2), ACTIVITY REGULATION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM
RP 2), ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAF63857.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAF63857.1};
RX PubMed=15901640; DOI=10.1095/biolreprod.104.039180;
RA Vasta V., Sonnenburg W.K., Yan C., Soderling S.H., Shimizu-Albergine M.,
RA Beavo J.A.;
RT "Identification of a new variant of PDE1A calmodulin-stimulated cyclic
RT nucleotide phosphodiesterase expressed in mouse sperm.";
RL Biol. Reprod. 73:598-609(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Yan C., Sonnenburg W.K., Zhao A.Z., Kwak K.S., Beavo J.A.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:BAC31606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31606.1};
RC TISSUE=Brain cortex {ECO:0000312|EMBL:BAC31606.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000312|EMBL:EDL27255.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-242 (ISOFORM 4).
RC TISSUE=Heart;
RA Sonnenburg W.K., Rybalkin S.D., Bornfeldt K.E., Kwak K.S., Rybalkina I.,
RA Beavo J.A.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium/calmodulin-dependent cyclic nucleotide
CC phosphodiesterase with a dual specificity for the second messengers
CC cGMP and cAMP, which are key regulators of many important physiological
CC processes. Has a higher efficiency with cGMP compared to cAMP.
CC {ECO:0000269|PubMed:15901640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC Evidence={ECO:0000269|PubMed:15901640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC Evidence={ECO:0000305|PubMed:15901640};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC Evidence={ECO:0000269|PubMed:15901640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC Evidence={ECO:0000305|PubMed:15901640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:15901640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000305|PubMed:15901640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15901640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:15901640};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:15901640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000305|PubMed:15901640};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15901640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:15901640};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q01064};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q01064};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q01064};
CC Note=Binds 2 divalent metal cations per subunit. Site 2 has a
CC preference for magnesium ions. {ECO:0000250|UniProtKB:Q01064};
CC -!- ACTIVITY REGULATION: Type I PDE are activated by the binding of
CC calmodulin in the presence of Ca(2+). {ECO:0000269|PubMed:15901640}.
CC -!- ACTIVITY REGULATION: [Isoform 2]: Activated by the binding of
CC calmodulin in the presence of Ca(2+). {ECO:0000269|PubMed:15901640}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with YWHAZ (By
CC similarity). {ECO:0000250|UniProtKB:P14100,
CC ECO:0000250|UniProtKB:P54750}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:15901640}. Note=Concentrates in the tail of mature
CC sperm. {ECO:0000269|PubMed:15901640}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Pde1a_v2 {ECO:0000303|PubMed:15901640}, mmPDE1A2
CC {ECO:0000303|PubMed:15901640};
CC IsoId=Q61481-4; Sequence=Displayed;
CC Name=2; Synonyms=Pde1a_v7 {ECO:0000303|PubMed:15901640}, mmPDE1A7
CC {ECO:0000303|PubMed:15901640};
CC IsoId=Q61481-5; Sequence=VSP_060311, VSP_060313, VSP_060314;
CC Name=3; Synonyms=Pde1a_v9 {ECO:0000303|PubMed:15901640}, mmPDE1A9
CC {ECO:0000303|PubMed:15901640};
CC IsoId=Q61481-6; Sequence=VSP_060311, VSP_060312, VSP_060315;
CC Name=4; Synonyms=PDE1A1, Pde1a_v1 {ECO:0000303|PubMed:15901640};
CC IsoId=Q61481-2; Sequence=VSP_004551;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney and testis.
CC {ECO:0000269|PubMed:15901640}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB03319.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF159298; AAF63857.1; -; mRNA.
DR EMBL; AY845864; AAW31879.1; -; mRNA.
DR EMBL; U56649; AAB03319.1; ALT_SEQ; mRNA.
DR EMBL; AK043647; BAC31606.1; -; mRNA.
DR EMBL; AL844577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27255.1; -; Genomic_DNA.
DR EMBL; CH466519; EDL27256.1; -; Genomic_DNA.
DR EMBL; CH466519; EDL27257.1; -; Genomic_DNA.
DR EMBL; BC090628; AAH90628.1; -; mRNA.
DR EMBL; AF023529; AAB81952.1; -; mRNA.
DR CCDS; CCDS16172.1; -. [Q61481-4]
DR CCDS; CCDS16173.1; -. [Q61481-5]
DR CCDS; CCDS16174.1; -. [Q61481-6]
DR RefSeq; NP_001009978.1; NM_001009978.1. [Q61481-5]
DR RefSeq; NP_001009979.1; NM_001009979.1. [Q61481-6]
DR RefSeq; NP_001153054.1; NM_001159582.1. [Q61481-4]
DR RefSeq; NP_058024.2; NM_016744.4. [Q61481-4]
DR RefSeq; XP_006498982.1; XM_006498919.3. [Q61481-4]
DR RefSeq; XP_006498983.1; XM_006498920.3.
DR RefSeq; XP_006498984.1; XM_006498921.3.
DR RefSeq; XP_006498986.1; XM_006498923.3.
DR AlphaFoldDB; Q61481; -.
DR SMR; Q61481; -.
DR BioGRID; 202074; 8.
DR IntAct; Q61481; 3.
DR MINT; Q61481; -.
DR STRING; 10090.ENSMUSP00000099711; -.
DR iPTMnet; Q61481; -.
DR PhosphoSitePlus; Q61481; -.
DR MaxQB; Q61481; -.
DR PaxDb; Q61481; -.
DR PeptideAtlas; Q61481; -.
DR PRIDE; Q61481; -.
DR ProteomicsDB; 294038; -. [Q61481-4]
DR ProteomicsDB; 294039; -. [Q61481-2]
DR ProteomicsDB; 337264; -.
DR ProteomicsDB; 340829; -.
DR ProteomicsDB; 344638; -.
DR Antibodypedia; 19750; 280 antibodies from 35 providers.
DR DNASU; 18573; -.
DR Ensembl; ENSMUST00000102651; ENSMUSP00000099711; ENSMUSG00000059173. [Q61481-6]
DR Ensembl; ENSMUST00000102652; ENSMUSP00000099712; ENSMUSG00000059173. [Q61481-5]
DR Ensembl; ENSMUST00000102653; ENSMUSP00000099713; ENSMUSG00000059173. [Q61481-4]
DR Ensembl; ENSMUST00000102654; ENSMUSP00000099714; ENSMUSG00000059173. [Q61481-4]
DR Ensembl; ENSMUST00000102655; ENSMUSP00000099715; ENSMUSG00000059173. [Q61481-4]
DR Ensembl; ENSMUST00000183775; ENSMUSP00000139327; ENSMUSG00000059173. [Q61481-4]
DR GeneID; 18573; -.
DR KEGG; mmu:18573; -.
DR UCSC; uc008khd.2; mouse. [Q61481-4]
DR UCSC; uc008khe.1; mouse.
DR UCSC; uc008khf.1; mouse.
DR CTD; 5136; -.
DR MGI; MGI:1201792; Pde1a.
DR VEuPathDB; HostDB:ENSMUSG00000059173; -.
DR eggNOG; KOG3688; Eukaryota.
DR GeneTree; ENSGT00940000157043; -.
DR HOGENOM; CLU_005940_1_5_1; -.
DR InParanoid; Q61481; -.
DR OMA; LFRRSNM; -.
DR OrthoDB; 904682at2759; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.17; 3474.
DR Reactome; R-MMU-111957; Cam-PDE 1 activation.
DR Reactome; R-MMU-418457; cGMP effects.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 18573; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Pde1a; mouse.
DR PRO; PR:Q61481; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61481; protein.
DR Bgee; ENSMUSG00000059173; Expressed in spermatid and 203 other tissues.
DR ExpressionAtlas; Q61481; baseline and differential.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004117; F:calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR InterPro; IPR013706; PDEase_N.
DR Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; cAMP; Cell projection; cGMP;
KW Cilium; Flagellum; Hydrolase; Magnesium; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..545
FT /note="Dual specificity calcium/calmodulin-dependent 3',5'-
FT cyclic nucleotide phosphodiesterase 1A"
FT /id="PRO_0000198786"
FT DOMAIN 142..522
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 24..44
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P14100"
FT REGION 114..137
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P14100"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT VAR_SEQ 1..71
FT /note="MGSTDTDIEELENATYKYLIGEQTEKMWQRLKGILRCLVKQLEKGDVNVVDL
FT KKNIEYAASVLEAVYIDET -> MIF (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000269|PubMed:15901640"
FT /id="VSP_060311"
FT VAR_SEQ 1..34
FT /note="MGSTDTDIEELENATYKYLIGEQTEKMWQRLKGI -> MDEYVTIRKKHLQR
FT PIFR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_004551"
FT VAR_SEQ 522..533
FT /note="GELDLHKNSEEL -> EPKSILQEQRCC (in isoform 3)"
FT /evidence="ECO:0000269|PubMed:15901640"
FT /id="VSP_060312"
FT VAR_SEQ 523..524
FT /note="EL -> CC (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:15901640"
FT /id="VSP_060313"
FT VAR_SEQ 525..545
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:15901640"
FT /id="VSP_060314"
FT VAR_SEQ 534..545
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000269|PubMed:15901640"
FT /id="VSP_060315"
SQ SEQUENCE 545 AA; 62347 MW; 5B794C8DE8456917 CRC64;
MGSTDTDIEE LENATYKYLI GEQTEKMWQR LKGILRCLVK QLEKGDVNVV DLKKNIEYAA
SVLEAVYIDE TRRLLDTEDE LSDIQTDSVP SEVRDWLAST FTRKMGMMKK KPEEKPKFRS
IVHAVQAGIF VERMYRKNYH MVGLTYPAAV IVTLKEVDKW SFDVFALNEA SGEHSLKFMI
YELFTRYDLI NRFKIPVSCL IAFAEALEVG YSKHKNPYHN LVHAADVTQT VHYIMLHTGI
MHWLTELEIL AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI LYNDRSVLEN HHVSAAYRLM
QEEEMNILVN LSKDDWRDLR NLVIEMVLAT DMSGHFQQIK NIRNSLQQPE GIDRAKTMSL
ILHAADISHP AKTWKLHYRW TMALMEEFFL QGDKEAELGL PFSPLCDRKS TMVAQSQIGF
IDFIVEPTFS LLTDSTEKIV IPLIEEASKS QSSNYGASSS STMIGFHVAD SLRRSNTKGS
VCDGSYAPDY SLSAVDLKSF KNNLVDIIQQ NKERWKELAA QGELDLHKNS EELGNTEEKH
ADTRP
