ID CUL9_MOUSE Reviewed; 1865 AA.
AC Q80TT8; Q8BKL9; Q8CGC0; Q8R363;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=Cullin-9;
DE Short=CUL-9;
DE AltName: Full=p53-associated parkin-like cytoplasmic protein;
GN Name=Cul9; Synonyms=Kiaa0708, Parc;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
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] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-1865 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=15964813; DOI=10.1128/mcb.25.13.5579-5589.2005;
RA Skaar J.R., Arai T., DeCaprio J.A.;
RT "Dimerization of CUL7 and PARC is not required for all CUL7 functions and
RT mouse development.";
RL Mol. Cell. Biol. 25:5579-5589(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Testis;
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).
RN [6]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21487039; DOI=10.1158/0008-5472.can-10-4300;
RA Pei X.H., Bai F., Li Z., Smith M.D., Whitewolf G., Jin R., Xiong Y.;
RT "Cytoplasmic CUL9/PARC ubiquitin ligase is a tumor suppressor and promotes
RT p53-dependent apoptosis.";
RL Cancer Res. 71:2969-2977(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RBX1 AND CUL7.
RX PubMed=24793696; DOI=10.1016/j.molcel.2014.03.046;
RA Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.;
RT "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin
RT to maintain genome integrity.";
RL Mol. Cell 54:805-819(2014).
CC -!- FUNCTION: Core component of a Cul9-RING ubiquitin-protein ligase
CC complex, a complex that mediates ubiquitination and subsequent
CC degradation of BIRC5 and is required to maintain microtubule dynamics
CC and genome integrity. Acts downstream of the 3M complex, which inhibits
CC CUL9 activity, leading to prevent ubiquitination of BIRC5
CC (PubMed:24793696). Cytoplasmic anchor protein in p53/TP53-associated
CC protein complex. Regulates the subcellular localization of p53/TP53 and
CC subsequent function. {ECO:0000269|PubMed:24793696}.
CC -!- SUBUNIT: Part of a Cul9-RING complex at least composed of CUL9 and
CC RBX1. Interacts with CUL7: interaction with CUL7 component of the 3M
CC complex leads to inhibition of CUL9 activity. The CUL7-CUL9 heterodimer
CC seems to interact specifically with TP53. Forms a complex with p53/TP53
CC in the cytoplasm of unstressed cells. Interacts with UBCH7 and UBCH8
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21487039}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80TT8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TT8-2; Sequence=VSP_009576;
CC Name=3;
CC IsoId=Q80TT8-3; Sequence=VSP_009577, VSP_009578;
CC Name=4;
CC IsoId=Q80TT8-4; Sequence=VSP_009579, VSP_009580;
CC -!- DOMAIN: The IBR domain is required for interaction with UBCH7 and
CC UBCH8.
CC -!- DISRUPTION PHENOTYPE: Mice were born at the expected Mendelian ratio
CC and do not show apparent phenotype. They are however more susceptible
CC to carcinogenesis and develop spontaneous tumor. Cells display
CC polyploidy and aneuploidy. {ECO:0000269|PubMed:15964813,
CC ECO:0000269|PubMed:21487039, ECO:0000269|PubMed:24793696}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK051474; Type=Frameshift; Evidence={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; AK051474; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC026469; AAH26469.1; -; mRNA.
DR EMBL; BC041674; AAH41674.1; -; mRNA.
DR EMBL; AK122351; BAC65633.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q80TT8; -.
DR SMR; Q80TT8; -.
DR STRING; 10090.ENSMUSP00000138418; -.
DR GlyGen; Q80TT8; 2 sites, 1 O-linked glycan (2 sites).
DR MaxQB; Q80TT8; -.
DR PaxDb; 10090-ENSMUSP00000138418; -.
DR PeptideAtlas; Q80TT8; -.
DR ProteomicsDB; 279298; -. [Q80TT8-1]
DR ProteomicsDB; 279299; -. [Q80TT8-2]
DR ProteomicsDB; 279300; -. [Q80TT8-3]
DR ProteomicsDB; 279301; -. [Q80TT8-4]
DR UCSC; uc008ctb.2; mouse. [Q80TT8-1]
DR UCSC; uc008ctf.2; mouse. [Q80TT8-3]
DR AGR; MGI:1925559; -.
DR MGI; MGI:1925559; Cul9.
DR eggNOG; KOG1815; Eukaryota.
DR InParanoid; Q80TT8; -.
DR PhylomeDB; Q80TT8; -.
DR ChiTaRS; Cul9; mouse.
DR PRO; PR:Q80TT8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TT8; Protein.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd20347; BRcat_RBR_CUL9; 1.
DR CDD; cd20359; Rcat_RBR_CUL9; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR047561; BRcat_RBR_CUL9.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047560; Rcat_RBR_CUL9.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22771:SF2; CULLIN-9; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1865
FT /note="Cullin-9"
FT /id="PRO_0000119816"
FT DOMAIN 480..659
FT /note="DOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT ZN_FING 1409..1459
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 1479..1542
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 1575..1604
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 265..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1622
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1778..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1794..1835
FT /evidence="ECO:0000255"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1841
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 700..707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1523
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 1618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWT3"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWT3"
FT MOD_RES 1775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWT3"
FT VAR_SEQ 1..908
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009576"
FT VAR_SEQ 134..144
FT /note="ALKMLAIANSS -> VSTLGRAGQSD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009577"
FT VAR_SEQ 145..1865
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009578"
FT VAR_SEQ 944..1009
FT /note="LLSLGSSWLEGAVLEQIGPCFPNRLPQLMLQSLHTSEELQHRFHLFQLQQLD
FT RQLLEQGDQEEWRP -> RLEENSLQTQDQPFPSWSCHRAAGRSPHCAICTTPESTYRR
FT SSAMPWSASPASTATVRSWGQEAGA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009579"
FT VAR_SEQ 1010..1865
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009580"
FT CONFLICT 1102
FT /note="L -> F (in Ref. 1; AK051474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104..1119
FT /note="Missing (in Ref. 3; BAC65633)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111..1119
FT /note="LNTVQMWLL -> TVQMWLLLN (in Ref. 1; AK051474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183
FT /note="F -> V (in Ref. 1; AK051474)"
FT /evidence="ECO:0000305"
FT CONFLICT 1592
FT /note="T -> N (in Ref. 1; AK051474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1865 AA; 209160 MW; 9956A32BE5BC5803 CRC64;
MARALRGPGP RSSLDQHVAA VLATVQISSL DTNLQLSGLC ALSQAVEEVT ERDHPLVRPD
RPLREKLVKT LVDLLTNQVG EKMVVVMALR LLYLLMTKHE WRPLFAREGG IYAVLICMQE
YKTSVLVQQA GLAALKMLAI ANSSDVPTFI PSRDSIQPLF DTQMTREIFA SIDSATRPGS
ESLLLSVPAA VVLMLNTEGC SSAVRNGLLL LNLLLCNHHT LGDQIITQEL RDTLFRHSGI
APGTEPMPTT RTILTMLLSR YSEPRGSPER AVLETPSTQG QDGSPESLIR SLVGDLSAEL
FLDLERVLCH EGSPPAAVRP LLRRLQQETQ PFLLLLRTLD APGPNRTLLL TILRVMTRLL
DHPETMVLPW HEVLEPCLNC LNGPSSDSEV VQEVTCFLHR LALMQKDYAV VLCCLGGKEA
LSKVLDKHST QLLLASELRH LVAECEKYSQ LCSNLTSSIL AGCIQMVLGQ IEDHRRTYKP
ITIPFFDVFL RHLCQGSSVE VKEDRCWEKV EVSSNPHRAS KLTDRNPKTY WESNGSTGSH
SITLHMHRGV LIRQLTLLVA SEDSSYMPAR VVVFGGDNVG CISTELNTVN VMPSASRVTL
LENLTRFWPI IQIRIKRCQQ GGIDTRVRGV EVLGPKPTFW PLFREQLCRR TCLFYTIRAQ
AWSRDIAEDR QRLLQLYPRL NRVLRHEQNF ADRFLPDDEA AQALGKTCWE ALVSPLVQNI
TSPDAGGVSS LGWLLDQYLE HRESTRSRQG PAASFASQVR RLCHLLVHVE APPGPSPEPS
SQPLSKNSKG QDGSPTPAPT PVCPSTSLRN LTQCWLSVVQ GQVSRFLAAA WRASDFVPRY
CSLYQRLQSA GSELFGPRAA FTLALRSGFS GALLQQSFLT AAHISEQFAR HIDQQIHGGL
LGGAAGVGML GRLQRHLEPI MVLSGLELAT TFEHFYQHYM ADRLLSLGSS WLEGAVLEQI
GPCFPNRLPQ LMLQSLHTSE ELQHRFHLFQ LQQLDRQLLE QGDQEEWRPE KVEEDDEGQE
TGRELFTDPG PAISVLVLSP RCWPVSPLCY LHHPRKHLQA ELCDALERFS SFYSHSQNCP
VLDIGPHRRL QWTWLGRAEL QLGDQTLHVS LNTVQMWLLF NQSEEVSVET LLRNSDLSPE
LLHQALLPLT SDNGPLTLEE TQDYPQGGVL RLREPRSQTH EEFLWLIPPQ TYLSVEKDEG
RTLEQKRNLL SCLLVRILKA HREKGLHIDQ LVCLVLEAWQ KGPDPPGRLG NAAAVGVACS
STDVLSCILH LLGQGYVERR DDRPQVLMYA TPEPMGPCRG QADVPFCGNK NTETSRPSPE
AVVALASLQL PAGRTMSPQE VEGLMEQTVR QVQETLNLEP DVAQHLLAHS HWGTEQLLQS
YSDDPEPLLL AAGLRVPQAQ VVPTRPDQCP VCVTPLGPHD DSPSLCCLHC CCKSCWNEYL
TTRIEQNFVL NCTCPIADCP AQPTGAFIRN IVSSPEVISK YEKALLRGYV ESCSNLTWCT
NPQGCDRILC RQGLGSGTTC SKCGWASCFS CSFPEAHYPA SCGHMSQWVD DGGYYDGMSV
EAQSKHLAKL ISKRCPSCQA PIEKNEGCLH MTCARCNHGF CWRCLKSWKP SHKDYYNCSA
MVSKAARQEK RFQDYNERCT FHHQAREFAV NLRNQASAIQ EVPPPKSFTF LQDACRALEQ
ARKVLAYACV YSFYSQDTEY MDVVEQQTEN LELHTNALQI LLEETLLRCR DLASSLRFLR
ADCLSTGTEL LRRIQERLLA ILQHSTQDFR VGLQSPSVET REVKGSNVPS DQPQGSSGLE
VEDEEEEEEE EEEEEEEEEE DVPEWQHEFD EELDNDSFSY DEESENLDRE TFFFGDEDED
DESYD
//
