PJA1_HUMAN
ID PJA1_HUMAN Reviewed; 643 AA.
AC Q8NG27; A2A322; Q5JUT8; Q5JUT9; Q8NG28; Q9HAC1;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=E3 ubiquitin-protein ligase Praja-1;
DE Short=Praja1;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 70;
DE AltName: Full=RING-type E3 ubiquitin transferase Praja-1 {ECO:0000305};
GN Name=PJA1; Synonyms=RNF70;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH UBE2D2.
RC TISSUE=Brain;
RX PubMed=12036302; DOI=10.1006/geno.2002.6770;
RA Yu P., Chen Y., Tagle D.A., Cai T.;
RT "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X
RT chromosome gene abundantly expressed in brain.";
RL Genomics 79:869-874(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-432
RP AND ASP-606.
RC TISSUE=Brain, Kidney, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-643 (ISOFORM 1).
RC TISSUE=Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND THR-277, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity.
CC Ubiquitinates MAGED1 antigen leading to its subsequent degradation by
CC proteasome (By similarity). May be involved in protein sorting.
CC {ECO:0000250, ECO:0000269|PubMed:12036302}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). In vitro, interacts
CC with the ubiquitin-conjugating enzyme, UBE2D2.
CC {ECO:0000269|PubMed:12036302}.
CC -!- INTERACTION:
CC Q8NG27; Q9Y5V3: MAGED1; NbExp=7; IntAct=EBI-714606, EBI-716006;
CC Q8NG27; Q96MG7: NSMCE3; NbExp=3; IntAct=EBI-714606, EBI-2557356;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NG27-1; Sequence=Displayed;
CC Name=2; Synonyms=PJA1-beta, Praja1-beta;
CC IsoId=Q8NG27-2; Sequence=VSP_007518;
CC Name=3;
CC IsoId=Q8NG27-3; Sequence=VSP_046995;
CC -!- TISSUE SPECIFICITY: Expressed in various regions of the brain including
CC the cerebellum, cerebral cortex, medulla, occipital pole, frontal lobe,
CC temporal lobe and putamen. Highest levels in the cerebral cortex.
CC {ECO:0000269|PubMed:12036302}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC -!- PTM: Substrate for E2-dependent ubiquitination.
CC -!- MISCELLANEOUS: [Isoform 2]: PubMed:12036302 reported that isoform 2
CC arises by alternative initiation. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13928.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF262024; AAM53039.1; -; mRNA.
DR EMBL; AF264620; AAM53040.1; -; mRNA.
DR EMBL; AL157699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05367.1; -; Genomic_DNA.
DR EMBL; BC048323; AAH48323.1; -; mRNA.
DR EMBL; BC075803; AAH75803.1; -; mRNA.
DR EMBL; BC105051; AAI05052.1; -; mRNA.
DR EMBL; BC105053; AAI05054.1; -; mRNA.
DR EMBL; AK021892; BAB13928.1; ALT_INIT; mRNA.
DR CCDS; CCDS14392.1; -. [Q8NG27-2]
DR CCDS; CCDS14393.1; -. [Q8NG27-1]
DR CCDS; CCDS35316.1; -. [Q8NG27-3]
DR RefSeq; NP_001027568.1; NM_001032396.2. [Q8NG27-3]
DR RefSeq; NP_071763.2; NM_022368.4. [Q8NG27-2]
DR RefSeq; NP_660095.1; NM_145119.3. [Q8NG27-1]
DR RefSeq; XP_005262349.1; XM_005262292.1.
DR RefSeq; XP_011529313.1; XM_011531011.2.
DR PDB; 2L0B; NMR; -; A=564-643.
DR PDBsum; 2L0B; -.
DR AlphaFoldDB; Q8NG27; -.
DR BMRB; Q8NG27; -.
DR SMR; Q8NG27; -.
DR BioGRID; 122109; 115.
DR IntAct; Q8NG27; 26.
DR STRING; 9606.ENSP00000355014; -.
DR iPTMnet; Q8NG27; -.
DR PhosphoSitePlus; Q8NG27; -.
DR BioMuta; PJA1; -.
DR DMDM; 31076980; -.
DR EPD; Q8NG27; -.
DR jPOST; Q8NG27; -.
DR MassIVE; Q8NG27; -.
DR MaxQB; Q8NG27; -.
DR PaxDb; Q8NG27; -.
DR PeptideAtlas; Q8NG27; -.
DR PRIDE; Q8NG27; -.
DR ProteomicsDB; 246; -.
DR ProteomicsDB; 73411; -. [Q8NG27-1]
DR ProteomicsDB; 73412; -. [Q8NG27-2]
DR Antibodypedia; 402; 164 antibodies from 32 providers.
DR DNASU; 64219; -.
DR Ensembl; ENST00000361478.1; ENSP00000355014.1; ENSG00000181191.12. [Q8NG27-1]
DR Ensembl; ENST00000374571.5; ENSP00000363699.3; ENSG00000181191.12. [Q8NG27-3]
DR Ensembl; ENST00000374583.1; ENSP00000363711.1; ENSG00000181191.12. [Q8NG27-1]
DR Ensembl; ENST00000374584.3; ENSP00000363712.3; ENSG00000181191.12. [Q8NG27-2]
DR GeneID; 64219; -.
DR KEGG; hsa:64219; -.
DR MANE-Select; ENST00000374571.5; ENSP00000363699.3; NM_001032396.4; NP_001027568.1. [Q8NG27-3]
DR UCSC; uc004dxg.4; human. [Q8NG27-1]
DR CTD; 64219; -.
DR DisGeNET; 64219; -.
DR GeneCards; PJA1; -.
DR HGNC; HGNC:16648; PJA1.
DR HPA; ENSG00000181191; Tissue enhanced (epididymis).
DR MIM; 300420; gene.
DR neXtProt; NX_Q8NG27; -.
DR OpenTargets; ENSG00000181191; -.
DR PharmGKB; PA33342; -.
DR VEuPathDB; HostDB:ENSG00000181191; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000154585; -.
DR HOGENOM; CLU_026830_1_0_1; -.
DR InParanoid; Q8NG27; -.
DR OMA; FNHDVRE; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q8NG27; -.
DR TreeFam; TF330711; -.
DR PathwayCommons; Q8NG27; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8NG27; -.
DR SIGNOR; Q8NG27; -.
DR BioGRID-ORCS; 64219; 11 hits in 743 CRISPR screens.
DR GeneWiki; PJA1; -.
DR GenomeRNAi; 64219; -.
DR Pharos; Q8NG27; Tbio.
DR PRO; PR:Q8NG27; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8NG27; protein.
DR Bgee; ENSG00000181191; Expressed in cortical plate and 191 other tissues.
DR ExpressionAtlas; Q8NG27; baseline and differential.
DR Genevisible; Q8NG27; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031227; PJA1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710:SF2; PTHR15710:SF2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..643
FT /note="E3 ubiquitin-protein ligase Praja-1"
FT /id="PRO_0000055999"
FT ZN_FING 595..636
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55176"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55176"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046995"
FT VAR_SEQ 98..285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12036302"
FT /id="VSP_007518"
FT VARIANT 432
FT /note="S -> N (in dbSNP:rs5937160)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052088"
FT VARIANT 606
FT /note="E -> D (in dbSNP:rs11539157)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052089"
FT HELIX 571..575
FT /evidence="ECO:0007829|PDB:2L0B"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:2L0B"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:2L0B"
FT TURN 596..598
FT /evidence="ECO:0007829|PDB:2L0B"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:2L0B"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:2L0B"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:2L0B"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:2L0B"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:2L0B"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:2L0B"
SQ SEQUENCE 643 AA; 71002 MW; F3DFD1F77809318D CRC64;
MGQESSKPVW PNPTGGYQSN TGRRYGRRHA YVSFRPPTSQ RERIASQRKT NSEVPMHRSA
PSQTTKRSRS PFSTTRRSWD DSESSGTNLN IDNEDYSRYP PREYRASGSR RGMAYGHIDS
YGADDSEEEG AGPVERPPVR GKTGKFKDDK LYDPEKGARS LAGPPPHFSS FSRDVREERD
KLDPVPAARC SASRADFLPQ SSVASQSSSE GKLATKGDSS ERERREQNLP ARPSRAPVSI
CGGGENTSKS AEEPVVRPKI RNLASPNCVK PKIFFDTDDD DDMPHSTSRW RDTANDNEGH
SDGLARRGRG ESSSGYPEPK YPEDKREARS DQVKPEKVPR RRRTMADPDF WTHSDDYYKY
CDEDSDSDKE WIAALRRKYR SREQTLSSSG ESWETLPGKE EREPPQAKVS ASTGTSPGPG
ASASAGAGAG ASAGSNGSNY LEEVREPSLQ EEQASLEEGE IPWLQYHEND SSSEGDNDSG
HELMQPGVFM LDGNNNLEDD SSVSEDLEVD WSLFDGFADG LGVAEAISYV DPQFLTYMAL
EERLAQAMET ALAHLESLAV DVEVANPPAS KESIDALPEI LVTEDHGAVG QEMCCPICCS
EYVKGEVATE LPCHHYFHKP CVSIWLQKSG TCPVCRCMFP PPL
