ID   ADCYA_MOUSE             Reviewed;        1614 AA.
AC   Q8C0T9; B2RRJ9; Q3V0F8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=Adenylate cyclase type 10;
DE            EC=4.6.1.1;
DE   AltName: Full=Germ cell soluble adenylyl cyclase;
DE            Short=sAC;
DE   AltName: Full=Testicular soluble adenylyl cyclase;
GN   Name=Adcy10; Synonyms=Sac, Sacy;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [3]
RP   ALTERNATIVE SPLICING.
RX   PubMed=11423534; DOI=10.1074/jbc.m011698200;
RA   Jaiswal B.S., Conti M.;
RT   "Identification and functional analysis of splice variants of the germ cell
RT   soluble adenylyl cyclase.";
RL   J. Biol. Chem. 276:31698-31708(2001).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12475901; DOI=10.1096/fj.02-0598fje;
RA   Zippin J.H., Chen Y., Nahirney P., Kamenetsky M., Wuttke M.S.,
RA   Fischman D.A., Levin L.R., Buck J.;
RT   "Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct
RT   signaling microdomains.";
RL   FASEB J. 17:82-84(2003).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14976244; DOI=10.1073/pnas.0400050101;
RA   Esposito G., Jaiswal B.S., Xie F., Krajnc-Franken M.A.M., Robben T.J.A.A.,
RA   Strik A.M., Kuil C., Philipsen R.L.A., van Duin M., Conti M., Gossen J.A.;
RT   "Mice deficient for soluble adenylyl cyclase are infertile because of a
RT   severe sperm-motility defect.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2993-2998(2004).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16054031; DOI=10.1016/j.devcel.2005.06.007;
RA   Hess K.C., Jones B.H., Marquez B., Chen Y., Ord T.S., Kamenetsky M.,
RA   Miyamoto C., Zippin J.H., Kopf G.S., Suarez S.S., Levin L.R.,
RA   Williams C.J., Buck J., Moss S.B.;
RT   "The 'soluble' adenylyl cyclase in sperm mediates multiple signaling events
RT   required for fertilization.";
RL   Dev. Cell 9:249-259(2005).
CC   -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP. May
CC       function as sensor that mediates responses to changes in cellular
CC       bicarbonate and CO(2) levels (By similarity). Has a critical role in
CC       mammalian spermatogenesis by producing the cAMP which regulates cAMP-
CC       responsive nuclear factors indispensable for sperm maturation in the
CC       epididymis. Induces capacitation, the maturational process that sperm
CC       undergo prior to fertilization (PubMed:14976244, PubMed:16054031).
CC       Involved in ciliary beat regulation (By similarity).
CC       {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:14976244,
CC       ECO:0000269|PubMed:16054031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC         Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q96PN6};
CC       Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC       (in vitro). {ECO:0000250|UniProtKB:Q96PN6};
CC   -!- ACTIVITY REGULATION: Activated by manganese or magnesium ions. In the
CC       presence of magnesium ions, the enzyme is activated by bicarbonate.
CC       Calcium mildly increases the enzyme activity, also in the presence of
CC       magnesium ions. {ECO:0000250|UniProtKB:Q96PN6}.
CC   -!- INTERACTION:
CC       Q8C0T9; Q6UJY2: Slc9c1; NbExp=2; IntAct=EBI-15639026, EBI-15639080;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96PN6};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q96PN6}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:12475901}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:12475901}. Nucleus {ECO:0000269|PubMed:12475901}.
CC       Cell projection, cilium {ECO:0000250|UniProtKB:Q96PN6}. Cytoplasm
CC       {ECO:0000269|PubMed:12475901}. Mitochondrion
CC       {ECO:0000269|PubMed:12475901}. Note=Distributed to subcellular
CC       compartments containing cAMP targets. Found as a plasma membrane-
CC       associated protein, protein concentrated in the perinuclear region and
CC       protein colocalized with actin or tubulin.
CC       {ECO:0000250|UniProtKB:Q96PN6, ECO:0000269|PubMed:12475901}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C0T9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0T9-2; Sequence=VSP_030871, VSP_030872;
CC   -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16054031}.
CC   -!- DOMAIN: The N-terminal guanylate cyclase domains are required for
CC       enzyme activity. Fragments containing the first 470 amino acid residues
CC       are fully active. {ECO:0000250|UniProtKB:Q96PN6}.
CC   -!- DISRUPTION PHENOTYPE: Mice are infertile because of a severe sperm-
CC       motility defect. {ECO:0000269|PubMed:14976244}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; AK029849; BAC26642.1; -; mRNA.
DR   EMBL; AK133181; BAE21546.1; -; mRNA.
DR   EMBL; BC138448; AAI38449.1; -; mRNA.
DR   CCDS; CCDS35756.1; -. [Q8C0T9-1]
DR   RefSeq; NP_766617.2; NM_173029.3. [Q8C0T9-1]
DR   RefSeq; XP_006496930.1; XM_006496867.1. [Q8C0T9-1]
DR   RefSeq; XP_017176545.1; XM_017321056.1. [Q8C0T9-1]
DR   AlphaFoldDB; Q8C0T9; -.
DR   SMR; Q8C0T9; -.
DR   BioGRID; 234845; 3.
DR   DIP; DIP-60950N; -.
DR   IntAct; Q8C0T9; 1.
DR   STRING; 10090.ENSMUSP00000027852; -.
DR   iPTMnet; Q8C0T9; -.
DR   PhosphoSitePlus; Q8C0T9; -.
DR   PaxDb; 10090-ENSMUSP00000027852; -.
DR   ProteomicsDB; 285765; -. [Q8C0T9-1]
DR   ProteomicsDB; 285766; -. [Q8C0T9-2]
DR   Antibodypedia; 3017; 185 antibodies from 24 providers.
DR   DNASU; 271639; -.
DR   Ensembl; ENSMUST00000027852.15; ENSMUSP00000027852.9; ENSMUSG00000026567.17. [Q8C0T9-1]
DR   Ensembl; ENSMUST00000148550.8; ENSMUSP00000137959.2; ENSMUSG00000026567.17. [Q8C0T9-2]
DR   GeneID; 271639; -.
DR   KEGG; mmu:271639; -.
DR   UCSC; uc007djf.1; mouse. [Q8C0T9-1]
DR   AGR; MGI:2660854; -.
DR   CTD; 55811; -.
DR   MGI; MGI:2660854; Adcy10.
DR   VEuPathDB; HostDB:ENSMUSG00000026567; -.
DR   eggNOG; ENOG502QPPT; Eukaryota.
DR   GeneTree; ENSGT00390000001322; -.
DR   HOGENOM; CLU_047661_0_0_1; -.
DR   InParanoid; Q8C0T9; -.
DR   OMA; HCRSGDF; -.
DR   OrthoDB; 3076794at2759; -.
DR   PhylomeDB; Q8C0T9; -.
DR   TreeFam; TF329284; -.
DR   BRENDA; 4.6.1.1; 3474.
DR   Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR   BioGRID-ORCS; 271639; 0 hits in 63 CRISPR screens.
DR   PRO; PR:Q8C0T9; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8C0T9; Protein.
DR   Bgee; ENSMUSG00000026567; Expressed in spermatid and 29 other cell types or tissues.
DR   ExpressionAtlas; Q8C0T9; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0097450; C:astrocyte end-foot; ISO:MGI.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0045178; C:basal part of cell; ISO:MGI.
DR   GO; GO:0090724; C:central region of growth cone; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0071890; F:bicarbonate binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR   GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0071241; P:cellular response to inorganic substance; ISS:UniProtKB.
DR   GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISS:UniProtKB.
DR   GO; GO:0006007; P:glucose catabolic process; ISO:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:1990544; P:mitochondrial ATP transmembrane transport; ISO:MGI.
DR   GO; GO:0106135; P:negative regulation of cardiac muscle cell contraction; ISO:MGI.
DR   GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR   GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR   GO; GO:1990535; P:neuron projection maintenance; ISO:MGI.
DR   GO; GO:0106028; P:neuron projection retraction; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR   GO; GO:0045819; P:positive regulation of glycogen catabolic process; ISO:MGI.
DR   GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR   GO; GO:0045778; P:positive regulation of ossification; ISO:MGI.
DR   GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR   GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR   GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR   GO; GO:1901524; P:regulation of mitophagy; ISO:MGI.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR   CDD; cd07302; CHD; 2.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR016577; Adenylate_cyclase_typ10.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR16305:SF32; ADENYLATE CYCLASE TYPE 10; 1.
DR   PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   PIRSF; PIRSF011131; Soluble_adenylyl_cyclase; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
DR   Genevisible; Q8C0T9; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane;
KW   Cell projection; Cytoplasm; Cytoskeleton; Lyase; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1614
FT                   /note="Adenylate cyclase type 10"
FT                   /id="PRO_0000317102"
FT   DOMAIN          42..179
FT                   /note="Guanylate cyclase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   DOMAIN          293..418
FT                   /note="Guanylate cyclase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         47..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         95
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         167
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         176
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         337
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   BINDING         412..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q96PN6"
FT   VAR_SEQ         470..471
FT                   /note="MF -> TC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030871"
FT   VAR_SEQ         472..1614
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030872"
FT   CONFLICT        304
FT                   /note="Q -> H (in Ref. 1; BAC26642)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1009
FT                   /note="I -> V (in Ref. 1; BAC26642)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1614 AA;  186412 MW;  AE56433825277126 CRC64;
     MSARRQELQD RAIVKIAAHL PDLIVYGDFS PERPSVKCFD GVLMFVDISG FTAMTEKFST
     AMYMDRGAEQ LVEILNYYIS AIVEKVLIFG GDILKFAGDA LLALWKVERK QLKNIITVVI
     KCSLEIHGLF EAKEAEEGLD IRVKIGLAAG HITMLVFGDE TRNYFLVIGQ AVDDVRLAQN
     MAQMNDVILS PNCWQLCDRS MIEIERIPDQ RAVKVSFLKP PPTFNFDEFF TKCMGFMDYY
     PSGDHKNFLR LACMLESDPE LELSLQKYVM EIILKQIDDK QLRGYLSELR PVTIVFVNLM
     FKEQDKVEVI GSAIQAACVH ITSVLKVFRG QINKVFMFDK GCSFLCVFGF PGEKAPDEIT
     HALESAVDIF DFCSQVHKIR TVSIGVASGI VFCGIVGHTV RHEYTVIGQK VNIAARMMMY
     YPGIVSCDSV TYDGSNLPAY FFKELPKKVM KGVADPGPVY QCLGLNEKVM FGMAYLICNR
     YEGYPLLGRV REIDYFMSTM KDFLMTNCSR VLMYEGLPGY GKSQVLMEIE YLASQHENHR
     AVAIALTKIS FHQNFYTIQI LMANVLGLDT CKHYKERQTN LQNRVKTLLD EKFHCLLNDI
     FHVQFPVSRE MSRMSKIRKQ KQLEALFMKI LAQTVREERI IFIIDEAQFV DGTSWAFIEK
     LIRSMPIFIV MSLAPFSEVP CAAANAIMKN RNTTYITLGT MQPQEIRDKV CVDLSVSSIP
     RELDSYLVEG SCGIPYYCEE LLKNLDHHRV LLFQQAETEQ KTNVTWNNMF KHSVRPTDDM
     QLFTSISEGQ KEVCYLVSGV RLNNLSPPAS LKEISLVQLD SMSLSHQMLV RCAAIIGLTF
     TTELLFEILP CWNMKMMIKA LATLVESNVF NCFRSSKDLQ LALKQNVPTF EVHYRSLALK
     LKEGLTYGEE EELREMEGEV VECRILRFCR PIMQKTAYEL WLKDQKKVLH LKCARFLEES
     AHRCNHCRNV DFIPYHHFIV DIRLNTLDMD TVKRMVTSQG FKIDEEEAIF SKSELPRKYK
     FPENLSITEI REKILHFFDN VILKMKSSPN DIIPLESCQC KELLQIVILP LAQHFVALEE
     NNKALYYFLE LASAYLILGD NYNAYMYLGE GERLLKSLTN EDSWSQTFEY ATFYSLKAEV
     CFNMGQMVLA KKMLRKALKL LNRMFPCNLL TLTFQMHVEK NRLSHFMNQH TQEGSVPGKK
     LAQLYLQASC FSLLWRIYSL NFFFHYKYYG HLAAMMEMNT SLETQNDFQI IKAYLDFSLY
     HHLAGYQGVW FKYEILVMEQ LLNLPLKGEA IEIMAYTADT LGHIKFLMGH LDLAIELGSR
     AHRMWSLLRN PNKYQMVLCR LSKPLFLKSR YKHLVQVLGW LWDLSVTEED IFSKAFFYFV
     CLDIMLYSGF IYRTFEECLE FIHHNEDNRI LKFQSGLLLG LYSCIAVWYA RLQEWDNFNK
     FSDRAKHLVT RRTPTVLYYE GISRYMEGQV LHLQKQIEEQ AENAQDSGVE ILKALETLVA
     QNTTGPVFYP RLYHLMAYVC ILMGDGHSCD FFLNTALELS ETHGNLLEKC WLSMSKEWWY
     SASELTGDQW LQTVLSLPSW DKIVSGKGGQ RKRSWSWFCP PNFSMVSWSQ PQCA
//