ID AT2A2_RABIT Reviewed; 1042 AA. AC P20647; P04192; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 04-NOV-2026, entry version 190. DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2; DE Short=SERCA2; DE Short=SR Ca(2+)-ATPase 2; DE EC=7.2.2.10; DE AltName: Full=Calcium pump 2; DE AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform; DE AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase; GN Name=ATP2A2; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Smooth muscle; RX PubMed=2523389; DOI=10.1016/s0021-9258(18)83540-2; RA Lytton J., Zarain-Herzberg A., Periasamy M., McLennan D.H.; RT "Molecular cloning of the mammalian smooth muscle sarco(endo)plasmic RT reticulum Ca2+-ATPase."; RL J. Biol. Chem. 264:7059-7065(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Smooth muscle; RX PubMed=2165260; DOI=10.1093/nar/18.13.4026; RA Khan I., Grover A.K.; RT "Cloning of internal Ca pump from rabbit stomach smooth muscle."; RL Nucleic Acids Res. 18:4026-4026(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=2993904; DOI=10.1038/316696a0; RA McLennan D.H., Brandl C.J., Korczak B., Green N.M.; RT "Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle RT sarcoplasmic reticulum, deduced from its complementary DNA sequence."; RL Nature 316:696-700(1985). CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of CC ATP coupled with the translocation of calcium from the cytosol to the CC sarcoplasmic reticulum lumen. Involved in autophagy in response to CC starvation. Upon interaction with VMP1 and activation, controls ER- CC isolation membrane contacts for autophagosome formation. Also modulates CC ER contacts with lipid droplets, mitochondria and endosomes (By CC similarity). In coordination with FLVCR2 mediates heme-stimulated CC switching from mitochondrial ATP synthesis to thermogenesis (By CC similarity). {ECO:0000250|UniProtKB:O55143, CC ECO:0000250|UniProtKB:P16615}. CC -!- FUNCTION: [Isoform 2]: Involved in the regulation of the CC contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated CC Ca(2+) signaling pathways via its interaction with TMEM64 which is CC critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS CC generation necessary for proper osteoclast generation. Association CC between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking CC for activation of NFATC1 and production of mitochondrial ROS, thereby CC triggering Ca(2+) signaling cascades that promote osteoclast CC differentiation and activation. {ECO:0000250|UniProtKB:O55143}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+); CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; EC=7.2.2.10; CC Evidence={ECO:0000250|UniProtKB:P16615}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; CC Evidence={ECO:0000250|UniProtKB:P16615}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P11607}; CC -!- ACTIVITY REGULATION: Has different conformational states with CC differential Ca2+ affinity. The E1 conformational state (active form) CC shows high Ca(2+) affinity, while the E2 state exhibits low Ca(2+) CC affinity. Binding of ATP allosterically increases its affinity for CC subsequent binding of Ca2+. Reversibly inhibited by phospholamban (PLN) CC at low calcium concentrations. PLN inhibits ATP2A2 Ca(2+) affinity by CC disrupting its allosteric activation by ATP. Inhibited by sarcolipin CC (SLN) and myoregulin (MRLN). The inhibition is blocked by VMP1. CC Enhanced by STRIT1/DWORF; STRIT1 increases activity by displacing CC sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN). Stabilizes CC SERCA2 in its E2 state. {ECO:0000250|UniProtKB:O46674, CC ECO:0000250|UniProtKB:O55143, ECO:0000250|UniProtKB:P04191, CC ECO:0000250|UniProtKB:P16615, ECO:0000250|UniProtKB:Q8R429}. CC -!- SUBUNIT: Interacts with sarcolipin (SLN); the interaction inhibits CC ATP2A2 Ca(2+) affinity. Interacts with phospholamban (PLN); the CC interaction inhibits ATP2A2 Ca(2+) affinity (By similarity). Interacts CC with myoregulin (MRLN) (By similarity). Interacts with ARLN and ERLN; CC the interactions inhibit ATP2A2 Ca(2+) affinity (By similarity). CC Interacts with SRTIT1/DWORF; the interaction results in activation of CC ATP2A2 (By similarity). Interacts with the monomeric forms of SLN, PLN, CC ARLN, ERLN and STRI1/DWORF (By similarity). Interacts with HAX1 (By CC similarity). Interacts with S100A8 and S100A9 (By similarity). CC Interacts with SLC35G1 and STIM1. Interacts with TMEM203 (By CC similarity). Interacts with TMEM64 and PDIA3 (By similarity). Interacts CC with TMX1 (By similarity). Interacts with TMX2 (By similarity). CC Interacts with VMP1; VMP1 competes with PLN and SLN to prevent them CC from forming an inhibitory complex with ATP2A2. Interacts with ULK1 (By CC similarity). Interacts with TUNAR (By similarity). Interacts with CC FLVCR2; this interaction occurs in the absence of heme and promotes CC ATP2A2 proteasomal degradation; this complex is dissociated upon heme CC binding. Interacts with FNIP1. {ECO:0000250|UniProtKB:O55143, CC ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615, CC ECO:0000250|UniProtKB:Q8R429}. CC -!- SUBUNIT: [Isoform 1]: Interacts with TRAM2 (via C-terminus). CC {ECO:0000250|UniProtKB:P16615}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein CC {ECO:0000255}. Sarcoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein CC {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER CC contact junction. {ECO:0000250|UniProtKB:O55143}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=ATP2A2B, SERCA2b; CC IsoId=P20647-1; Sequence=Displayed; CC Name=2; Synonyms=ATP2A2A, SERCA2a; CC IsoId=P20647-2; Sequence=VSP_000361; CC -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in heart and slow CC twitch skeletal muscle. Isoform 1 is widely expressed. CC -!- DOMAIN: Ca(2+) and ATP binding cause major rearrangements of the CC cytoplasmic and transmembrane domains. According to the E1-E2 model, CC Ca(2+) binding to the cytosolic domain of the pump in the high-affinity CC E1 conformation is followed by the ATP-dependent phosphorylation of the CC active site Asp, giving rise to E1P. A conformational change of the CC phosphoenzyme gives rise to the low-affinity E2P state that exposes the CC Ca(2+) ions to the lumenal side and promotes Ca(2+) release. CC Dephosphorylation of the active site Asp mediates the subsequent return CC to the E1 conformation. {ECO:0000250|UniProtKB:P04191}. CC -!- DOMAIN: PLN and SLN both have a single transmembrane helix; both occupy CC a similar binding site on ATP2A1 that is situated between the ATP2A1 CC transmembrane helices. {ECO:0000250|UniProtKB:P04191}. CC -!- PTM: Nitrated under oxidative stress. Nitration on the two tyrosine CC residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}. CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, CC leading to its inactivation. {ECO:0000250|UniProtKB:O55143}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIA subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04703; AAA31150.1; -; mRNA. DR EMBL; X52496; CAA36737.1; -; mRNA. DR EMBL; X02814; CAA26583.1; -; mRNA. DR PIR; A01076; PWRBSC. DR PIR; A33881; A33881. DR PIR; S10335; PWRBMC. DR RefSeq; NP_001082790.1; NM_001089321.1. DR AlphaFoldDB; P20647; -. DR SMR; P20647; -. DR FunCoup; P20647; 1516. DR STRING; 9986.ENSOCUP00000038801; -. DR PaxDb; 9986-ENSOCUP00000038801; -. DR GeneID; 100038308; -. DR KEGG; ocu:100038308; -. DR CTD; 488; -. DR eggNOG; KOG0202; Eukaryota. DR InParanoid; P20647; -. DR OMA; AACCLPI; -. DR OrthoDB; 3352408at2759; -. DR BRENDA; 7.2.2.10; 1749. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-ARBA. DR GO; GO:0005388; F:P-type calcium transporter activity; ISS:UniProtKB. DR GO; GO:0086039; F:P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential; ISS:UniProtKB. DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB. DR GO; GO:0016240; P:autophagosome membrane docking; ISS:UniProtKB. DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IEA:UniProtKB-ARBA. DR GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0003012; P:muscle system process; IEA:UniProtKB-ARBA. DR GO; GO:0008016; P:regulation of heart contraction; IEA:UniProtKB-ARBA. DR GO; GO:0006937; P:regulation of muscle contraction; IEA:UniProtKB-ARBA. DR CDD; cd02083; P-type_ATPase_SERCA; 1. DR FunFam; 3.40.1110.10:FF:000003; Calcium-transporting ATPase; 1. DR FunFam; 3.40.50.1000:FF:000005; Calcium-transporting ATPase 1; 1. DR FunFam; 1.20.1110.10:FF:000027; Calcium-transporting ATPase, putative; 1. DR FunFam; 1.20.1110.10:FF:000077; ECA1 (ER-TYPE CA2+-ATPASE 1); 1. DR FunFam; 1.20.1110.10:FF:000065; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C. DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N. DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf. DR InterPro; IPR059000; ATPase_P-type_domA. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR005782; P-type_ATPase_IIA. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 2. DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF08282; Hydrolase_3; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00120; HATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Calcium; Calcium transport; KW Disulfide bond; Endoplasmic reticulum; Ion transport; Magnesium; Membrane; KW Metal-binding; Nitration; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Sarcoplasmic reticulum; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1042 FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 2" FT /id="PRO_0000046199" FT TOPO_DOM 1..48 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 49..69 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 70..89 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 90..110 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 111..253 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 254..273 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 274..295 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 296..313 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 314..756 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 757..776 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 777..786 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 787..807 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 808..827 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 828..850 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 851..896 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 897..916 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 917..929 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 930..948 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 949..963 FT /note="Lumenal" FT /evidence="ECO:0000305" FT TRANSMEM 964..984 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P04191" FT TOPO_DOM 985..1042 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 575..594 FT /note="Interaction with HAX1" FT /evidence="ECO:0000250" FT REGION 787..807 FT /note="Interaction with PLN" FT /evidence="ECO:0000250|UniProtKB:P04191" FT REGION 788..1042 FT /note="Interaction with TMEM64 and PDIA3" FT /evidence="ECO:0000250|UniProtKB:O55143" FT REGION 931..942 FT /note="Interaction with PLN" FT /evidence="ECO:0000250|UniProtKB:P04191" FT ACT_SITE 351 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 304 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 305 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 307 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 309 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 351 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 353 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 442 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 489 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 514 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 559 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 624 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 625 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 626 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 677 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 683 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P04191" FT BINDING 702 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 705 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 767 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 770 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 795 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 798 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 799 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 799 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11607" FT BINDING 907 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P04191" FT MOD_RES 38 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O55143" FT MOD_RES 294 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P16615" FT MOD_RES 295 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P16615" FT MOD_RES 441 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q64578" FT MOD_RES 531 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O55143" FT MOD_RES 580 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16615" FT MOD_RES 663 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P16615" FT DISULFID 875..887 FT /evidence="ECO:0000250|UniProtKB:P11607" FT VAR_SEQ 994..1042 FT /note="GKECVQPAPQSCSLWACTEGVSWPFVLLIVPLVMWVYSTDTNFSDLLWS -> FT AILE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:2993904" FT /id="VSP_000361" FT CONFLICT 578 FT /note="K -> E (in Ref. 1; AAA31150)" FT /evidence="ECO:0000305" SQ SEQUENCE 1042 AA; 114705 MW; 4243836D67431575 CRC64; MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ MSVCRMFILD KVDGDTCSLN EFTITGSTYA PIGEVHKDDK PVKCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTAGV KQKIMSVIRE WGSGSDTLRC LALATHDNPL RREEMHLKDS ANFIKYETNL TFVGCVGMLD PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQEEDVTAK AFTGREFDEL NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP APQSCSLWAC TEGVSWPFVL LIVPLVMWVY STDTNFSDLL WS //