PROM1_MOUSE
ID PROM1_MOUSE Reviewed; 867 AA.
AC O54990; O35408; Q80XB2; Q80XB3; Q80XB6; Q8BH12;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Prominin-1;
DE AltName: Full=Antigen AC133 homolog;
DE AltName: Full=Prominin-like protein 1;
DE AltName: CD_antigen=CD133;
DE Flags: Precursor;
GN Name=Prom1; Synonyms=Prom, Proml1;
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 [MRNA] (ISOFORM 1).
RX PubMed=9389721;
RA Miraglia S., Godfrey W., Yin A.H., Atkins K., Warnke R., Holden J.T.,
RA Bray R.A., Waller E.K., Buck D.W.;
RT "A novel five-transmembrane hematopoietic stem cell antigen: isolation,
RT characterization, and molecular cloning.";
RL Blood 90:5013-5021(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=9356465; DOI=10.1073/pnas.94.23.12425;
RA Weigmann A., Corbeil D., Hellwig A., Huttner W.B.;
RT "Prominin, a novel microvilli-specific polytopic membrane protein of the
RT apical surface of epithelial cells, is targeted to plasmalemmal protrusions
RT of non-epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12425-12430(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=15316084; DOI=10.1242/jcs.01315;
RA Fargeas C.A., Joester A., Missol-Kolka E., Hellwig A., Huttner W.B.,
RA Corbeil D.;
RT "Identification of novel Prominin-1/CD133 splice variants with alternative
RT C-termini and their expression in epididymis and testis.";
RL J. Cell Sci. 117:4301-4311(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP SUBCELLULAR LOCATION, AND CHOLESTEROL BINDING.
RX PubMed=10980698; DOI=10.1038/35023524;
RA Roeper K., Corbeil D., Huttner W.B.;
RT "Retention of prominin in microvilli reveals distinct cholesterol-based
RT lipid micro-domains in the apical plasma membrane.";
RL Nat. Cell Biol. 2:582-592(2000).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12514187; DOI=10.1074/jbc.m210640200;
RA Fargeas C.A., Florek M., Huttner W.B., Corbeil D.;
RT "Characterization of prominin-2, a new member of the prominin family of
RT pentaspan membrane glycoproteins.";
RL J. Biol. Chem. 278:8586-8596(2003).
RN [7]
RP NOMENCLATURE OF ISOFORMS.
RX PubMed=17498271; DOI=10.1111/j.1399-0039.2007.00825.x;
RA Fargeas C.A., Huttner W.B., Corbeil D.;
RT "Nomenclature of prominin-1 (CD133) splice variants - an update.";
RL Tissue Antigens 69:602-606(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17109118; DOI=10.1007/s00441-006-0324-z;
RA Florek M., Bauer N., Janich P., Wilsch-Braeuninger M., Fargeas C.A.,
RA Marzesco A.-M., Ehninger G., Thiele C., Huttner W.B., Corbeil D.;
RT "Prominin-2 is a cholesterol-binding protein associated with apical and
RT basolateral plasmalemmal protrusions in polarized epithelial cells and
RT released into urine.";
RL Cell Tissue Res. 328:31-47(2007).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=17874118; DOI=10.1007/s00418-007-0334-2;
RA Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., Corbeil D.;
RT "Differential expression of prominin-1 (CD133) and prominin-2 in major
RT cephalic exocrine glands of adult mice.";
RL Histochem. Cell Biol. 128:409-419(2007).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=17283184; DOI=10.1083/jcb.200608137;
RA Dubreuil V., Marzesco A.M., Corbeil D., Huttner W.B.,
RA Wilsch-Braeuninger M.;
RT "Midbody and primary cilium of neural progenitors release extracellular
RT membrane particles enriched in the stem cell marker prominin-1.";
RL J. Cell Biol. 176:483-495(2007).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=18654668; DOI=10.1172/jci35891;
RA Yang Z., Chen Y., Lillo C., Chien J., Yu Z., Michaelides M., Klein M.,
RA Howes K.A., Li Y., Kaminoh Y., Chen H., Zhao C., Chen Y., Al-Sheikh Y.T.,
RA Karan G., Corbeil D., Escher P., Kamaya S., Li C., Johnson S.,
RA Frederick J.M., Zhao Y., Wang C., Cameron D.J., Huttner W.B.,
RA Schorderet D.F., Munier F.L., Moore A.T., Birch D.G., Baehr W., Hunt D.M.,
RA Williams D.S., Zhang K.;
RT "Mutant prominin 1 found in patients with macular degeneration disrupts
RT photoreceptor disk morphogenesis in mice.";
RL J. Clin. Invest. 118:2908-2916(2008).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19228982; DOI=10.1523/jneurosci.2034-08.2009;
RA Zacchigna S., Oh H., Wilsch-Brauninger M., Missol-Kolka E., Jaszai J.,
RA Jansen S., Tanimoto N., Tonagel F., Seeliger M., Huttner W.B., Corbeil D.,
RA Dewerchin M., Vinckier S., Moons L., Carmeliet P.;
RT "Loss of the cholesterol-binding protein prominin-1/CD133 causes disk
RT dysmorphogenesis and photoreceptor degeneration.";
RL J. Neurosci. 29:2297-2308(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-273; ASN-291 AND ASN-374.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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: May play a role in cell differentiation, proliferation and
CC apoptosis. Binds cholesterol in cholesterol-containing plasma membrane
CC microdomains and may play a role in the organization of the apical
CC plasma membrane in epithelial cells. During early retinal development
CC acts as a key regulator of disk morphogenesis (PubMed:19228982).
CC Involved in regulation of MAPK and Akt signaling pathways. In
CC neuroblastoma cells suppresses cell differentiation such as neurite
CC outgrowth in a RET-dependent manner. {ECO:0000269|PubMed:19228982}.
CC -!- SUBUNIT: Interacts with CDHR1 and with actin filaments. Interacts with
CC NAT8 and NAT8B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane
CC protein. Cell projection, microvillus membrane; Multi-pass membrane
CC protein. Cell projection, cilium, photoreceptor outer segment.
CC Endoplasmic reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250}. Note=Found in extracellular
CC membrane particles in various body fluids such as ventricular fluid of
CC the developing brain and urine.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=S2;
CC IsoId=O54990-1; Sequence=Displayed;
CC Name=2; Synonyms=S1;
CC IsoId=O54990-2; Sequence=VSP_040006;
CC Name=3; Synonyms=S3;
CC IsoId=O54990-3; Sequence=VSP_040006, VSP_040010, VSP_040011;
CC Name=4; Synonyms=S4;
CC IsoId=O54990-4; Sequence=VSP_040005, VSP_040007, VSP_040010,
CC VSP_040011;
CC Name=5; Synonyms=S5;
CC IsoId=O54990-5; Sequence=VSP_040006, VSP_040007, VSP_040010,
CC VSP_040011;
CC Name=6; Synonyms=S6;
CC IsoId=O54990-6; Sequence=VSP_040006, VSP_040008, VSP_040009;
CC -!- TISSUE SPECIFICITY: In the submandibular gland, expressed on the apical
CC side of epithelial cells. In the parotid gland, expressed in the
CC intercalated ducts. In the sublingual gland, expressed in intercalated
CC ducts. In the extraorbital lacrimal gland, expressed in the
CC intercalated tubules and larger intralobular ducts. Expressed in the
CC retina. Present in urine within small membrane particles (at protein
CC level). In the embryo, expressed on the apical side of neuroepithelial
CC cells and of other epithelia such as lung buds, gut and ureter buds. In
CC the adult, expressed at the apical side of the kidney tubules and of
CC the ependymal layer of the brain. Not expressed in gut, liver, lung,
CC pituitary, adrenal, heart or spleen. Localized to the nascent disk
CC membranes at the base of the rod outer segment in the retina (at
CC protein level). {ECO:0000269|PubMed:12514187,
CC ECO:0000269|PubMed:17874118, ECO:0000269|PubMed:18654668,
CC ECO:0000269|PubMed:19228982}.
CC -!- DEVELOPMENTAL STAGE: At birth, is detected at the interface between the
CC developing neuroretina and the retinal pigment epithelium (RPE) layer.
CC In the postnatal retina (P20) detected in photoreceptors, with
CC particular concentration in the region of plasma membrane evaginations
CC at the basal part of the outer segment (OS). Expressed by rod and cone
CC photoreceptor cells, most abundantly between the OS and inner segment
CC (IS), in close proximity to the connecting cilium.
CC {ECO:0000269|PubMed:19228982}.
CC -!- PTM: Acetylation at Lys-226, Lys-258 and Lys-265 by NAT8 and NAT8B may
CC control PROM1 protein expression and its function in cell apoptosis.
CC -!- DISRUPTION PHENOTYPE: Progressive degeneration and functional
CC deterioration of both cone and rod photoreceptors associated with
CC impaired morphogenesis of the disks and OS.
CC {ECO:0000269|PubMed:19228982}.
CC -!- MISCELLANEOUS: Fundus images and light microscopy of retinal sections
CC from transgenic mice expressing mutant PROM1 reveal progressive retinal
CC abnormalities visible as subretinal deposits and photoreceptor atrophy.
CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}.
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DR EMBL; AF039663; AAB96916.1; -; mRNA.
DR EMBL; AF026269; AAB86715.1; -; mRNA.
DR EMBL; AF305215; AAO11840.1; -; mRNA.
DR EMBL; AY099088; AAM28245.1; -; mRNA.
DR EMBL; AY223521; AAO72429.1; -; mRNA.
DR EMBL; AY223522; AAO72430.1; -; mRNA.
DR EMBL; AK030027; BAC26745.1; -; mRNA.
DR CCDS; CCDS39082.1; -. [O54990-2]
DR CCDS; CCDS51491.1; -. [O54990-5]
DR CCDS; CCDS51493.1; -. [O54990-3]
DR CCDS; CCDS51494.1; -. [O54990-1]
DR CCDS; CCDS80275.1; -. [O54990-4]
DR PIR; T08881; T08881.
DR RefSeq; NP_001157050.1; NM_001163578.1.
DR RefSeq; NP_001157053.1; NM_001163581.1.
DR RefSeq; NP_001157054.1; NM_001163582.1.
DR RefSeq; NP_001157055.1; NM_001163583.1.
DR AlphaFoldDB; O54990; -.
DR BioGRID; 202393; 1.
DR STRING; 10090.ENSMUSP00000073751; -.
DR GlyGen; O54990; 8 sites.
DR iPTMnet; O54990; -.
DR PhosphoSitePlus; O54990; -.
DR jPOST; O54990; -.
DR MaxQB; O54990; -.
DR PaxDb; O54990; -.
DR PeptideAtlas; O54990; -.
DR PRIDE; O54990; -.
DR ProteomicsDB; 291882; -. [O54990-1]
DR ProteomicsDB; 291883; -. [O54990-2]
DR ProteomicsDB; 291884; -. [O54990-3]
DR ProteomicsDB; 291885; -. [O54990-4]
DR ProteomicsDB; 291886; -. [O54990-5]
DR ProteomicsDB; 291887; -. [O54990-6]
DR DNASU; 19126; -.
DR GeneID; 19126; -.
DR KEGG; mmu:19126; -.
DR UCSC; uc008xii.1; mouse. [O54990-4]
DR CTD; 8842; -.
DR MGI; MGI:1100886; Prom1.
DR eggNOG; KOG4331; Eukaryota.
DR InParanoid; O54990; -.
DR PhylomeDB; O54990; -.
DR BioGRID-ORCS; 19126; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Prom1; mouse.
DR PRO; PR:O54990; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O54990; protein.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0071914; C:prominosome; IDA:UniProtKB.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IMP:UniProtKB.
DR GO; GO:0072139; P:glomerular parietal epithelial cell differentiation; ISO:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI.
DR GO; GO:0072112; P:podocyte differentiation; ISO:MGI.
DR GO; GO:2000768; P:positive regulation of nephron tubule epithelial cell differentiation; ISO:MGI.
DR GO; GO:0010842; P:retina layer formation; IMP:UniProtKB.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISO:MGI.
DR InterPro; IPR008795; Prominin.
DR PANTHER; PTHR22730; PTHR22730; 1.
DR Pfam; PF05478; Prominin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..867
FT /note="Prominin-1"
FT /id="PRO_0000025814"
FT TOPO_DOM 20..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..794
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 816..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 226
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43490"
FT MOD_RES 258
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43490"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43490"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43490"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 94..107
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15316084"
FT /id="VSP_040005"
FT VAR_SEQ 94..102
FT /note="Missing (in isoform 2, isoform 3, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15316084,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9356465"
FT /id="VSP_040006"
FT VAR_SEQ 335..360
FT /note="QLPSVDRELNTVTEVDKTDLESLVKR -> Q (in isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15316084"
FT /id="VSP_040007"
FT VAR_SEQ 832
FT /note="D -> E (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15316084"
FT /id="VSP_040008"
FT VAR_SEQ 833..867
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15316084"
FT /id="VSP_040009"
FT VAR_SEQ 833..843
FT /note="VETVPMKNLEI -> SSVSGMWHFTL (in isoform 3, isoform 4
FT and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15316084,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_040010"
FT VAR_SEQ 844..867
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15316084,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_040011"
FT CONFLICT 64
FT /note="S -> N (in Ref. 2; AAB86715, 3; AAM28245/AAO11840/
FT AAO72429/AAO72430 and 4; BAC26745)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="K -> N (in Ref. 2; AAB86715, 3; AAM28245/AAO11840/
FT AAO72429/AAO72430 and 4; BAC26745)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="P -> L (in Ref. 2; AAB86715, 3; AAM28245/AAO72429/
FT AAO72430 and 4; BAC26745)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="G -> D (in Ref. 2; AAB86715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 867 AA; 97113 MW; D442F6372552B3C8 CRC64;
MALVFSALLL LGLCGKISSE GQPAFHNTPG AMNYELPTTK YETQDTFNAG IVGPLYKMVH
IFLSVVQPND FPLDLIKKLI QNKKFDISVD SKEPEIIVLA LKIALYEIGV LICAILGLLF
IILMPLVGCF FCMCRCCNKC GGEMHQRQKQ NAPCRRKCLG LSLLVICLLM SLGIIYGFVA
NQQTRTRIKG TQKLAKSNFR DFQTLLTETP KQIDYVVEQY TNTKNKAFSD LDGIGSVLGG
RIKDQLKPKV TPVLEEIKAM ATAIKQTKDA LQNMSSSLKS LQDAATQLNT NLSSVRNSIE
NSLSSSDCTS DPASKICDSI RPSLSSLGSS LNSSQLPSVD RELNTVTEVD KTDLESLVKR
GYTTIDEIPN TIQNQTVDVI KDVKNTLDSI SSNIKDMSQS IPIEDMLLQV SHYLNNSNRY
LNQELPKLEE YDSYWWLGGL IVCFLLTLIV TFFFLGLLCG VFGYDKHATP TRRGCVSNTG
GIFLMAGVGF GFLFCWILMI LVVLTFVVGA NVEKLLCEPY ENKKLLQVLD TPYLLKEQWQ
FYLSGMLFNN PDINMTFEQV YRDCKRGRGI YAAFQLENVV NVSDHFNIDQ ISENINTELE
NLNVNIDSIE LLDNTGRKSL EDFAHSGIDT IDYSTYLKET EKSPTEVNLL TFASTLEAKA
NQLPEGKPKQ AFLLDVQNIR AIHQHLLPPV QQSLNTLRQS VWTLQQTSNK LPEKVKKILA
SLDSVQHFLT NNVSLIVIGE TKKFGKTILG YFEHYLHWVF YAITEKMTSC KPMATAMDSA
VNGILCGYVA DPLNLFWFGI GKATVLLLPA VIIAIKLAKY YRRMDSEDVY DDVETVPMKN
LEIGSNGYHK DHLYGVHNPV MTSPSRY
