KIRR3_MOUSE
ID KIRR3_MOUSE Reviewed; 778 AA.
AC Q8BR86; Q6P555; Q810H3; Q8BGQ5; Q8BRS8;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Kin of IRRE-like protein 3 {ECO:0000305};
DE AltName: Full=Kin of irregular chiasm-like protein 3;
DE AltName: Full=Nephrin-like protein 2 {ECO:0000303|PubMed:26283919};
DE AltName: Full=mKirre {ECO:0000303|PubMed:12665856};
DE Contains:
DE RecName: Full=Processed kin of IRRE-like protein 3;
DE Flags: Precursor;
GN Name=Kirrel3; Synonyms=Kiaa1867, Neph2 {ECO:0000303|PubMed:26283919};
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 4), PROTEIN CLEAVAGE, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12665856; DOI=10.1038/ni916;
RA Ueno H., Sakita-Ishikawa M., Morikawa Y., Nakano T., Kitamura T., Saito M.;
RT "A stromal cell-derived membrane protein that supports hematopoietic stem
RT cells.";
RL Nat. Immunol. 4:457-463(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Corpora quadrigemina;
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 2).
RC STRAIN=C57BL/6J; 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 SUBUNIT, INTERACTION WITH NPHS1, AND PROTEIN CLEAVAGE.
RX PubMed=15843475; DOI=10.1681/asn.2004060439;
RA Gerke P., Sellin L., Kretz O., Petraschka D., Zentgraf H., Benzing T.,
RA Walz G.;
RT "NEPH2 is located at the glomerular slit diaphragm, interacts with nephrin
RT and is cleaved from podocytes by metalloproteinases.";
RL J. Am. Soc. Nephrol. 16:1693-1702(2005).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15908127; DOI=10.1016/j.neuroscience.2005.03.030;
RA Tamura S., Morikawa Y., Hisaoka T., Ueno H., Kitamura T., Senba E.;
RT "Expression of mKirre, a mammalian homolog of Drosophila kirre, in the
RT developing and adult mouse brain.";
RL Neuroscience 133:615-624(2005).
RN [6]
RP TISSUE SPECIFICITY, AND INTERACTION WITH NPHS1.
RX PubMed=18752272; DOI=10.1002/cne.21838;
RA Komori T., Gyobu H., Ueno H., Kitamura T., Senba E., Morikawa Y.;
RT "Expression of kin of irregular chiasm-like 3/mKirre in proprioceptive
RT neurons of the dorsal root ganglia and its interaction with nephrin in
RT muscle spindles.";
RL J. Comp. Neurol. 511:92-108(2008).
RN [7]
RP FUNCTION.
RX PubMed=21241806; DOI=10.1016/j.mcn.2011.01.007;
RA Nishida K., Nakayama K., Yoshimura S., Murakami F.;
RT "Role of Neph2 in pontine nuclei formation in the developing hindbrain.";
RL Mol. Cell. Neurosci. 46:662-670(2011).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23637329; DOI=10.1242/dev.087262;
RA Prince J.E., Brignall A.C., Cutforth T., Shen K., Cloutier J.F.;
RT "Kirrel3 is required for the coalescence of vomeronasal sensory neuron
RT axons into glomeruli and for male-male aggression.";
RL Development 140:2398-2408(2013).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26575286; DOI=10.7554/elife.09395;
RA Martin E.A., Muralidhar S., Wang Z., Cervantes D.C., Basu R., Taylor M.R.,
RA Hunter J., Cutforth T., Wilke S.A., Ghosh A., Williams M.E.;
RT "The intellectual disability gene Kirrel3 regulates target-specific mossy
RT fiber synapse development in the hippocampus.";
RL Elife 4:0-0(2015).
RN [10]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26283919; DOI=10.3389/fncel.2015.00283;
RA Choi S.Y., Han K., Cutforth T., Chung W., Park H., Lee D., Kim R.,
RA Kim M.H., Choi Y., Shen K., Kim E.;
RT "Mice lacking the synaptic adhesion molecule Neph2/Kirrel3 display moderate
RT hyperactivity and defective novel object preference.";
RL Front. Cell. Neurosci. 9:283-283(2015).
CC -!- FUNCTION: Synaptic adhesion molecule required for the formation of
CC target-specific synapses (PubMed:23637329, PubMed:26575286). Required
CC for formation of target-specific synapses at hippocampal mossy fiber
CC synapses. Required for formation of mossy fiber filopodia, the synaptic
CC structures connecting dentate granule and GABA neurons. Probably acts
CC as a homophilic adhesion molecule that promotes trans-cellular
CC interactions and stabilize mossy fiber filipodia contact and subsequent
CC synapse formation (PubMed:26575286). Required for the coalescence of
CC vomeronasal sensory neuron axons (PubMed:23637329). May be involved in
CC the hematopoietic supportive capacity of stroma cells; the secreted
CC extracellular domain is directly responsible for supporting
CC hematopoietic stem cells (PubMed:12665856).
CC {ECO:0000269|PubMed:12665856, ECO:0000269|PubMed:23637329,
CC ECO:0000269|PubMed:26575286}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion (PubMed:26575286). Interacts with NPHS1; forms heterodimers
CC with NPHS1 (PubMed:15843475, PubMed:18752272). Interacts with
CC NPHS2/podocin (via the C-terminus) (By similarity). Interacts with
CC CASK. Interacts (via extracellular region) with MAP1B. Interacts (via
CC extracellular region) with MYO16. Interacts (via intracellular region)
CC with ATP1B1. Interacts (via intracellular region) with SHMT2. Interacts
CC (via intracellular region) with UFC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IZU9, ECO:0000269|PubMed:15843475,
CC ECO:0000269|PubMed:18752272, ECO:0000269|PubMed:26575286}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12665856};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12665856}. Cell
CC projection, axon {ECO:0000269|PubMed:26575286}. Cell projection,
CC dendrite {ECO:0000269|PubMed:26575286}.
CC -!- SUBCELLULAR LOCATION: [Processed kin of IRRE-like protein 3]: Secreted
CC {ECO:0000269|PubMed:12665856}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BR86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BR86-2; Sequence=VSP_011816, VSP_011818;
CC Name=3;
CC IsoId=Q8BR86-3; Sequence=VSP_011817, VSP_011819, VSP_011820;
CC Name=4;
CC IsoId=Q8BR86-4; Sequence=VSP_011817;
CC -!- TISSUE SPECIFICITY: Expressed mainly in adult brain, bone marrow and
CC stromal cells (PubMed:12665856). Expressed in diverse regions of the
CC brain, including the cortex, hippocampus, striatum, olfactory bulb and
CC cerebellum (PubMed:15908127, PubMed:26283919). In brain, expressed in
CC pontine nucleus neurons (at protein level) (PubMed:21241806). In
CC hippocampus, produced in both the dentate granule neurons and the
CC GABAergic neurons, but not the CA3 neurons (PubMed:26575286). Expressed
CC in subpopulations of vomeronasal sensory neurons (PubMed:23637329).
CC Expressed in a subset of neurons in dorsal root ganglia
CC (PubMed:18752272). {ECO:0000269|PubMed:12665856,
CC ECO:0000269|PubMed:15908127, ECO:0000269|PubMed:18752272,
CC ECO:0000269|PubMed:21241806, ECO:0000269|PubMed:23637329,
CC ECO:0000269|PubMed:26283919, ECO:0000269|PubMed:26575286}.
CC -!- DEVELOPMENTAL STAGE: At embryonic day 11.5, it is expressed in the
CC differentiating zones of various regions, such as the caudate-putamen,
CC the geniculate body, the thalamus, the amygdala and the brainstem. This
CC expression persists in the adult, although expression is lower. After
CC birth, highly expressed in the glomerular and mitral layers of the
CC olfactory bulb, the cortical plate of the neocortex, the cochlear
CC nucleus, and the molecular and granule cell layers of the cerebellum.
CC In the hippocampus, expression is first observed in the dentate gyrus
CC at postnatal day 7. {ECO:0000269|PubMed:15908127}.
CC -!- PTM: Undergoes proteolysis by a metalloprotease and gives rise to a
CC soluble form. {ECO:0000269|PubMed:12665856,
CC ECO:0000269|PubMed:15843475}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and their size is normal. Mice
CC show defects of the accessory olfactory system characterized by
CC disorganization of the glomerular layer of the posterior accessory
CC olfactory bulb and formation of fewer, larger glomeruli. Mice display a
CC loss of male-male aggression in a resident-intruder assay
CC (PubMed:23637329). Mice display moderate hyperactivity in a familiar,
CC but not novel, environment and defective novel object recognition with
CC normal performances in Morris water maze spatial learning and memory,
CC contextual fear conditioning and extinction, and pattern separation
CC tests (PubMed:26283919). Young mutant mice form fewer synapse-forming
CC structures between dentate granule neurons and GABAergic neurons than
CC normal mice, while the synapses that connect dentate granule neurons to
CC CA3 neurons form normally. This may affect the balance of activity
CC across the two types of dentate granule synapses and the CA3 neurons,
CC leading to hyperactivity (PubMed:26575286).
CC {ECO:0000269|PubMed:23637329, ECO:0000269|PubMed:26283919,
CC ECO:0000269|PubMed:26575286}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AY169782; AAO41835.1; -; mRNA.
DR EMBL; AK034142; BAC28604.1; -; mRNA.
DR EMBL; AK038385; BAC29980.1; -; mRNA.
DR EMBL; AK043580; BAC31587.1; -; mRNA.
DR EMBL; AK045373; BAC32333.1; -; mRNA.
DR EMBL; BC063072; AAH63072.1; -; mRNA.
DR CCDS; CCDS40574.1; -. [Q8BR86-4]
DR CCDS; CCDS80973.1; -. [Q8BR86-2]
DR RefSeq; NP_001177840.1; NM_001190911.1. [Q8BR86-1]
DR RefSeq; NP_001177841.1; NM_001190912.1. [Q8BR86-2]
DR RefSeq; NP_001177842.1; NM_001190913.1. [Q8BR86-3]
DR RefSeq; NP_080600.1; NM_026324.3. [Q8BR86-4]
DR RefSeq; XP_006510623.1; XM_006510560.3. [Q8BR86-1]
DR RefSeq; XP_006510624.1; XM_006510561.3. [Q8BR86-2]
DR RefSeq; XP_006510626.1; XM_006510563.3. [Q8BR86-4]
DR PDB; 7LU6; X-ray; 1.95 A; A/B/C/D/E/F/G/H=47-146.
DR PDBsum; 7LU6; -.
DR AlphaFoldDB; Q8BR86; -.
DR SASBDB; Q8BR86; -.
DR SMR; Q8BR86; -.
DR BioGRID; 212378; 2.
DR STRING; 10090.ENSMUSP00000140219; -.
DR GlyConnect; 2452; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BR86; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BR86; -.
DR PhosphoSitePlus; Q8BR86; -.
DR PaxDb; Q8BR86; -.
DR PRIDE; Q8BR86; -.
DR ProteomicsDB; 263546; -. [Q8BR86-1]
DR ProteomicsDB; 263547; -. [Q8BR86-2]
DR ProteomicsDB; 263548; -. [Q8BR86-3]
DR ProteomicsDB; 263549; -. [Q8BR86-4]
DR ABCD; Q8BR86; 2 sequenced antibodies.
DR Antibodypedia; 33010; 144 antibodies from 30 providers.
DR DNASU; 67703; -.
DR Ensembl; ENSMUST00000115148; ENSMUSP00000110801; ENSMUSG00000032036. [Q8BR86-4]
DR Ensembl; ENSMUST00000187182; ENSMUSP00000140219; ENSMUSG00000032036. [Q8BR86-2]
DR GeneID; 67703; -.
DR KEGG; mmu:67703; -.
DR UCSC; uc009osg.1; mouse. [Q8BR86-3]
DR UCSC; uc009osh.2; mouse. [Q8BR86-4]
DR UCSC; uc009osi.2; mouse. [Q8BR86-1]
DR UCSC; uc009osj.2; mouse. [Q8BR86-2]
DR CTD; 84623; -.
DR MGI; MGI:1914953; Kirrel3.
DR VEuPathDB; HostDB:ENSMUSG00000032036; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000157126; -.
DR InParanoid; Q8BR86; -.
DR OMA; LMVEHEE; -.
DR OrthoDB; 269917at2759; -.
DR PhylomeDB; Q8BR86; -.
DR TreeFam; TF327139; -.
DR Reactome; R-MMU-373753; Nephrin family interactions.
DR BioGRID-ORCS; 67703; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Kirrel3; mouse.
DR PRO; PR:Q8BR86; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BR86; protein.
DR Bgee; ENSMUSG00000032036; Expressed in cortical plate and 151 other tissues.
DR ExpressionAtlas; Q8BR86; baseline and differential.
DR Genevisible; Q8BR86; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; NAS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0072102; P:glomerulus morphogenesis; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IDA:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0021740; P:principal sensory nucleus of trigeminal nerve development; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..778
FT /note="Kin of IRRE-like protein 3"
FT /id="PRO_0000015099"
FT CHAIN 22..?
FT /note="Processed kin of IRRE-like protein 3"
FT /evidence="ECO:0000305|PubMed:12665856"
FT /id="PRO_0000296241"
FT TOPO_DOM 22..535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..142
FT /note="Ig-like C2-type 1"
FT DOMAIN 147..243
FT /note="Ig-like C2-type 2"
FT DOMAIN 249..330
FT /note="Ig-like C2-type 3"
FT DOMAIN 335..415
FT /note="Ig-like C2-type 4"
FT DOMAIN 419..515
FT /note="Ig-like C2-type 5"
FT REGION 727..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 271..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 356..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 440..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 19..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011816"
FT VAR_SEQ 518..529
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12665856,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011817"
FT VAR_SEQ 565
FT /note="R -> RSTGGRPGISGRGTEKKARLRLPRRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011818"
FT VAR_SEQ 603..624
FT /note="MDRGEFQQDSVLKQLEVLKEEE -> VRAQPMPHSILSTQTSRCSPYC (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011819"
FT VAR_SEQ 625..778
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011820"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:7LU6"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7LU6"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7LU6"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:7LU6"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7LU6"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:7LU6"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:7LU6"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:7LU6"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:7LU6"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:7LU6"
SQ SEQUENCE 778 AA; 85405 MW; D8DBEC8C096B4F81 CRC64;
MRPFQLDLLF LCFFLFSQEL GLQKRGCCLV LGYMAKDKFR RMNEGQVYSF SQQPQDQVVV
SGQPVTLLCA IPEYDGFVLW IKDGLALGVG RDLSSYPQYL VVGNHLSGEH HLKILRAELQ
DDAVYECQAI QAAIRSRPAR LTVLVPPDDP IILGGPVISL RAGDPLNLTC HADNAKPAAS
IIWLRKGEVI NGATYSKTLL RDGKRESIVS TLFISPGDVE NGQSIVCRAT NKAIPGGKET
SVTIDIQHPP LVNLSVEPQP VLEDNIVTFH CSAKANPAVT QYRWAKRGHI IKEASGELYR
TTVDYTYFSE PVSCEVTNAL GSTNLSRTVD VYFGPRMTSE PQSLLVDLGS DAVFSCAWIG
NPSLTIVWMK RGSGVVLSNE KTLTLKSVRQ EDAGKYVCRA VVPRVGAGER EVTLTVNGPP
IISSTQTQHA LHGEKGQIKC FIRSTPPPDR IAWSWKENVL ESGTSGRYTV ETVNTEEGVI
STLTISNIVR ADFQTIYNCT AWNSFGSDTE IIRLKEQGSE MKSGAGLEAE SVPMAVIIGV
AVGAGVAFLV LMATIVAFCC ARSQRNLKGV VSAKNDIRVE IVHKEPSSGR EAEDHTTIKQ
LMMDRGEFQQ DSVLKQLEVL KEEEKEFQNL KDPTNGYYSV NTFKEHHSTP TISLSSCQPD
LRPTGKQRVP TGMSFTNIYS TLSGQGRLYD YGQRFVLGMG SSSIELCERE FQRGSLSDSS
SFLDTQCDSS VSSSGKQDGY VQFDKASKAS ASSSHHSQSS SQNSDPSRPL QRRMQTHV
