NECT3_MOUSE
ID NECT3_MOUSE Reviewed; 549 AA.
AC Q9JLB9; Q059N7; Q9D006; Q9JLB7; Q9JLB8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Nectin-3;
DE AltName: Full=Nectin cell adhesion molecule 3 {ECO:0000250|UniProtKB:Q9NQS3};
DE AltName: Full=Poliovirus receptor-related protein 3;
DE AltName: CD_antigen=CD113;
DE Flags: Precursor;
GN Name=Nectin3 {ECO:0000250|UniProtKB:Q9NQS3}; Synonyms=Pvrl3;
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] (ISOFORMS 1; 2 AND 3), SUBUNIT, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M.,
RA Tachibana K., Mizoguchi A., Takai Y.;
RT "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that
RT shows homophilic and heterophilic cell-cell adhesion activities.";
RL J. Biol. Chem. 275:10291-10299(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12121624; DOI=10.1016/s0960-9822(02)00922-3;
RA Ozaki-Kuroda K., Nakanishi H., Ohta H., Tanaka H., Kurihara H., Mueller S.,
RA Irie K., Ikeda W., Sakai T., Wimmer E., Nishimune Y., Takai Y.;
RT "Nectin couples cell-cell adhesion and the actin scaffold at heterotypic
RT testicular junctions.";
RL Curr. Biol. 12:1145-1150(2002).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11827984; DOI=10.1083/jcb.200103113;
RA Mizoguchi A., Nakanishi H., Kimura K., Matsubara K., Ozaki-Kuroda K.,
RA Katata T., Honda T., Kiyohara Y., Heo K., Higashi M., Tsutsumi T.,
RA Sonoda S., Ide C., Takai Y.;
RT "Nectin: an adhesion molecule involved in formation of synapses.";
RL J. Cell Biol. 156:555-565(2002).
RN [6]
RP FUNCTION.
RX PubMed=12558799; DOI=10.1046/j.1365-2443.2003.00616.x;
RA Honda T., Shimizu K., Kawakatsu T., Yasumi M., Shingai T., Fukuhara A.,
RA Ozaki-Kuroda K., Irie K., Nakanishi H., Takai Y.;
RT "Antagonistic and agonistic effects of an extracellular fragment of nectin
RT on formation of E-cadherin-based cell-cell adhesion.";
RL Genes Cells 8:51-63(2003).
RN [7]
RP INTERACTION WITH IGSF4.
RX PubMed=12826663; DOI=10.1074/jbc.m305387200;
RA Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
RA Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
RT "Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in
RT cell-cell adhesion and transmembrane protein localization in epithelial
RT cells.";
RL J. Biol. Chem. 278:35421-35427(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH PVR.
RX PubMed=16128743; DOI=10.1111/j.1349-7006.2005.00087.x;
RA Sato T., Irie K., Okamoto R., Ooshio T., Fujita N., Takai Y.;
RT "Common signaling pathway is used by the trans-interaction of Necl-
RT 5/Tage4/PVR/CD155 and nectin, and of nectin and nectin during the formation
RT of cell-cell adhesion.";
RL Cancer Sci. 96:578-589(2005).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=15728677; DOI=10.1242/dev.01697;
RA Inagaki M., Irie K., Ishizaki H., Tanaka-Okamoto M., Morimoto K., Inoue E.,
RA Ohtsuka T., Miyoshi J., Takai Y.;
RT "Roles of cell-adhesion molecules nectin 1 and nectin 3 in ciliary body
RT development.";
RL Development 132:1525-1537(2005).
RN [10]
RP INTERACTION WITH IGSF4B.
RX PubMed=15741237; DOI=10.1242/jcs.01656;
RA Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T.,
RA Mizoguchi A., Takai Y.;
RT "Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific
RT immunoglobulin-like cell-cell adhesion molecule localizing at non-
RT junctional contact sites of presynaptic nerve terminals, axons and glia
RT cell processes.";
RL J. Cell Sci. 118:1267-1277(2005).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=16300961; DOI=10.1016/j.mcn.2005.10.002;
RA Honda T., Sakisaka T., Yamada T., Kumazawa N., Hoshino T., Kajita M.,
RA Kayahara T., Ishizaki H., Tanaka-Okamoto M., Mizoguchi A., Manabe T.,
RA Miyoshi J., Takai Y.;
RT "Involvement of nectins in the formation of puncta adherentia junctions and
RT the mossy fiber trajectory in the mouse hippocampus.";
RL Mol. Cell. Neurosci. 31:315-325(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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).
CC -!- FUNCTION: Plays a role in cell-cell adhesion through heterophilic
CC trans-interactions with nectins-like or other nectins, such as trans-
CC interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-
CC interaction with PVR induces activation of CDC42 and RAC small G
CC proteins through common signaling molecules such as SRC and RAP1. Also
CC involved in the formation of cell-cell junctions, including adherens
CC junctions and synapses. Induces endocytosis-mediated down-regulation of
CC PVR from the cell surface, resulting in reduction of cell movement and
CC proliferation. Plays a role in the morphology of the ciliary body.
CC {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984,
CC ECO:0000269|PubMed:12121624, ECO:0000269|PubMed:12558799,
CC ECO:0000269|PubMed:16128743}.
CC -!- SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers with
CC NECTIN1, NECTIN2, PVR, IGSF4B/Necl-1 and with IGSF4. Interaction
CC between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites,
CC respectively, initiates the formation of puncta adherentia junctions
CC between axons and dendrites. Interacts (via Cytoplasmic domain) with
CC AFDN, providing a connection with the actin cytoskeleton. Binds with
CC low affinity to TIGIT. {ECO:0000269|PubMed:10744716,
CC ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:12826663,
CC ECO:0000269|PubMed:15741237, ECO:0000269|PubMed:16128743}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:11827984}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Nectin-3 alpha;
CC IsoId=Q9JLB9-1; Sequence=Displayed;
CC Name=2; Synonyms=Nectin-3 beta;
CC IsoId=Q9JLB9-2; Sequence=VSP_017437, VSP_017440;
CC Name=3; Synonyms=Nectin-3 gamma;
CC IsoId=Q9JLB9-3; Sequence=VSP_017438, VSP_017439;
CC -!- TISSUE SPECIFICITY: Ubiquitous with high expression in testes.
CC Localized in spermatids at Sertoli-spermatid junctions. Expressed in
CC ovarian granulosa cells, but only faintly expressed after ovulation.
CC {ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:12121624}.
CC -!- DISRUPTION PHENOTYPE: Mice show an ocular phenotype, microphthalmia,
CC accompanied by a separation of the contact between the pigment and non-
CC pigment cell layers of the ciliary epithelia. Male mice exhibits
CC infertility, suggesting a role in spermatogenesis. In the hippocampus,
CC the formation and the number of adherens junctions at the synapses is
CC impaired, and the trajectory of mossy fiber is abnormal.
CC {ECO:0000269|PubMed:15728677, ECO:0000269|PubMed:16300961}.
CC -!- SIMILARITY: Belongs to the nectin family. {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; AF195833; AAF63685.1; -; mRNA.
DR EMBL; AF195834; AAF63686.1; -; mRNA.
DR EMBL; AF195835; AAF63687.1; -; mRNA.
DR EMBL; AK011949; BAB27933.1; -; mRNA.
DR EMBL; BC125588; AAI25589.1; -; mRNA.
DR EMBL; BC132187; AAI32188.1; -; mRNA.
DR CCDS; CCDS28204.1; -. [Q9JLB9-2]
DR CCDS; CCDS28205.1; -. [Q9JLB9-3]
DR CCDS; CCDS28206.1; -. [Q9JLB9-1]
DR RefSeq; NP_067470.1; NM_021495.4. [Q9JLB9-1]
DR RefSeq; NP_067471.1; NM_021496.3. [Q9JLB9-2]
DR RefSeq; NP_067472.1; NM_021497.2. [Q9JLB9-3]
DR PDB; 3AXA; X-ray; 2.78 A; A/B=544-549.
DR PDB; 5B22; X-ray; 2.58 A; A/B=59-266.
DR PDBsum; 3AXA; -.
DR PDBsum; 5B22; -.
DR AlphaFoldDB; Q9JLB9; -.
DR SMR; Q9JLB9; -.
DR BioGRID; 208471; 1.
DR DIP; DIP-41729N; -.
DR IntAct; Q9JLB9; 2.
DR MINT; Q9JLB9; -.
DR STRING; 10090.ENSMUSP00000023334; -.
DR GlyGen; Q9JLB9; 6 sites.
DR iPTMnet; Q9JLB9; -.
DR PhosphoSitePlus; Q9JLB9; -.
DR MaxQB; Q9JLB9; -.
DR PaxDb; Q9JLB9; -.
DR PeptideAtlas; Q9JLB9; -.
DR PRIDE; Q9JLB9; -.
DR ProteomicsDB; 286174; -. [Q9JLB9-1]
DR ProteomicsDB; 286175; -. [Q9JLB9-2]
DR ProteomicsDB; 286176; -. [Q9JLB9-3]
DR Antibodypedia; 2646; 354 antibodies from 35 providers.
DR DNASU; 58998; -.
DR Ensembl; ENSMUST00000023334; ENSMUSP00000023334; ENSMUSG00000022656. [Q9JLB9-1]
DR Ensembl; ENSMUST00000023335; ENSMUSP00000023335; ENSMUSG00000022656. [Q9JLB9-2]
DR Ensembl; ENSMUST00000096052; ENSMUSP00000093757; ENSMUSG00000022656. [Q9JLB9-3]
DR GeneID; 58998; -.
DR KEGG; mmu:58998; -.
DR UCSC; uc007zji.3; mouse. [Q9JLB9-2]
DR UCSC; uc007zjj.2; mouse. [Q9JLB9-3]
DR UCSC; uc007zjk.3; mouse. [Q9JLB9-1]
DR CTD; 25945; -.
DR MGI; MGI:1930171; Nectin3.
DR VEuPathDB; HostDB:ENSMUSG00000022656; -.
DR eggNOG; ENOG502QTRU; Eukaryota.
DR GeneTree; ENSGT00940000156028; -.
DR HOGENOM; CLU_029618_3_0_1; -.
DR InParanoid; Q9JLB9; -.
DR OMA; QMYPLYS; -.
DR OrthoDB; 509401at2759; -.
DR PhylomeDB; Q9JLB9; -.
DR TreeFam; TF331051; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
DR BioGRID-ORCS; 58998; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Nectin3; mouse.
DR PRO; PR:Q9JLB9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JLB9; protein.
DR Bgee; ENSMUSG00000022656; Expressed in seminiferous tubule of testis and 260 other tissues.
DR ExpressionAtlas; Q9JLB9; baseline and differential.
DR Genevisible; Q9JLB9; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC-UCL.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:1902414; P:protein localization to cell junction; IDA:MGI.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR033319; Nectin-3.
DR PANTHER; PTHR23277:SF12; PTHR23277:SF12; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..57
FT /evidence="ECO:0000255"
FT CHAIN 58..549
FT /note="Nectin-3"
FT /id="PRO_0000226373"
FT TOPO_DOM 58..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..165
FT /note="Ig-like V-type"
FT DOMAIN 170..258
FT /note="Ig-like C2-type 1"
FT DOMAIN 269..354
FT /note="Ig-like C2-type 2"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 193..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 291..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 358..510
FT /note="PPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLKDDTIGTIIASV
FT VGGALFLVLVSILAGVFCYRRRRTFRGDYFAKNYIPPSDMQKESQIDVLHQDELDSYPD
FT SVKKENKNPVNNLIRKDYLEEPEKTQWNNVENLTRFERPMDY -> IPLTQTSSIAVAG
FT AVIGAVLALFIITVFVTVLLTPRKKRPSYLDKVIDLPPTHKPPPVYEERIPSLPQKDLL
FT GQTEHLPLQTQFKEKGAGGLQPSNGPISRRFDYEDESTMQEDGTQRMCPLYSQMCHQDR
FT SPRQHHPRNPERLYINPREHYV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10744716"
FT /id="VSP_017437"
FT VAR_SEQ 358..438
FT /note="PPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLKDDTIGTIIASV
FT VGGALFLVLVSILAGVFCYRRRRTFRGDY -> IPLTQTSSIAVAGAVIGAVLALFIIT
FT VFVTVLLTPRKKRPSYLDKVIDLPPTHKPPPVYEERIPSLPQKDLLGQVRALEDT (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10744716,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017438"
FT VAR_SEQ 439..549
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10744716,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017439"
FT VAR_SEQ 511..549
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10744716"
FT /id="VSP_017440"
FT CONFLICT 181
FT /note="L -> S (in Ref. 2; BAB27933)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..196
FT /note="AA -> SS (in Ref. 2; BAB27933)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..221
FT /note="MESSTTSFP -> REFSTISFL (in Ref. 2; BAB27933)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="K -> E (in Ref. 2; BAB27933)"
FT /evidence="ECO:0000305"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 83..95
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:5B22"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:5B22"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5B22"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 156..168
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5B22"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:5B22"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:5B22"
SQ SEQUENCE 549 AA; 60583 MW; 5492C9ABB472F185 CRC64;
MARTPGPAPL CPGGGKAQLS SAFPPAAGLL LPAPTPPPLL LLLIPLLLFS RLCGALAGSI
IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSTQ TVAVHHPQYG FSVQGDYQGR
VLFKNYSLND ATITLHNIGF SDSGKYICKA VTFPLGNAQS STTVTVLVEP TVSLIKGPDS
LIDGGNETVA AVCVAATGKP VAQIDWEGDL GEMESSTTSF PNETATIVSQ YKLFPTRFAR
GRRITCVVKH PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF
KSVWSRLDGQ WPDGLLASDN TLHFVHPLTV NYSGVYVCKV SNSLGQRSDQ KVIYISDPPT
TTTLQPTVQW HSSPADVQDI ATEHKKLPFP LSTLATLKDD TIGTIIASVV GGALFLVLVS
ILAGVFCYRR RRTFRGDYFA KNYIPPSDMQ KESQIDVLHQ DELDSYPDSV KKENKNPVNN
LIRKDYLEEP EKTQWNNVEN LTRFERPMDY YEDLKMGMKF VSDERYNESE DGLVSHVDGS
VISRREWYV
