NTNG1_MOUSE
ID NTNG1_MOUSE Reviewed; 539 AA.
AC Q8R4G0; Q68FE5; Q69ZU3; Q8R4F3; Q8R4F4; Q8R4F5; Q8R4F6; Q8R4F7; Q8R4F8;
AC Q8R4F9; Q9ESR3; Q9ESR4; Q9ESR5; Q9ESR6; Q9ESR7; Q9ESR8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Netrin-G1;
DE AltName: Full=Laminet-1;
DE Flags: Precursor;
GN Name=Ntng1; Synonyms=Kiaa0976, Lmnt1;
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 {ECO:0000312|EMBL:BAB12010.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 1E AND 1F),
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB12010.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAB12010.1};
RX PubMed=10964959; DOI=10.1523/jneurosci.20-17-06540.2000;
RA Nakashiba T., Ikeda T., Nishimura S., Tashiro K., Honjo T., Culotti J.G.,
RA Itohara S.;
RT "Netrin-G1: a novel glycosyl phosphatidylinositol-linked mammalian netrin
RT that is functionally divergent from classical netrins.";
RL J. Neurosci. 20:6540-6550(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 1E; 1F; 1G; 1H; 1I AND
RP 1J), AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:11906208};
RX PubMed=11906208; DOI=10.1006/mcne.2001.1089;
RA Yin Y., Miner J.H., Sanes J.R.;
RT "Laminets: laminin- and netrin-related genes expressed in distinct neuronal
RT subsets.";
RL Mol. Cell. Neurosci. 19:344-358(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1E).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1C).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1C).
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 [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11804778; DOI=10.1016/s0925-4773(01)00600-1;
RA Nakashiba T., Nishimura S., Ikeda T., Itohara S.;
RT "Complementary expression and neurite outgrowth activity of netrin-G
RT subfamily members.";
RL Mech. Dev. 111:47-60(2002).
RN [7]
RP FUNCTION.
RX PubMed=31692205; DOI=10.1002/humu.23945;
RA Heimer G., van Woerden G.M., Barel O., Marek-Yagel D., Kol N.,
RA Munting J.B., Borghei M., Atawneh O.M., Nissenkorn A., Rechavi G.,
RA Anikster Y., Elgersma Y., Kushner S.A., Ben Zeev B.;
RT "Netrin-G2 dysfunction causes a Rett-like phenotype with areflexia.";
RL Hum. Mutat. 41:476-486(2020).
CC -!- FUNCTION: Involved in controlling patterning and neuronal circuit
CC formation at the laminar, cellular, subcellular and synaptic levels.
CC Promotes neurite outgrowth of both axons and dendrites.
CC {ECO:0000269|PubMed:11804778, ECO:0000269|PubMed:31692205}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10964959};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10964959}; Extracellular
CC side {ECO:0000269|PubMed:10964959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1A {ECO:0000269|PubMed:11906208}; Synonyms=G1a
CC {ECO:0000269|PubMed:10964959};
CC IsoId=Q8R4G0-1; Sequence=Displayed;
CC Name=1B {ECO:0000269|PubMed:11906208}; Synonyms=G1b
CC {ECO:0000269|PubMed:10964959};
CC IsoId=Q8R4G0-2; Sequence=VSP_050547, VSP_050548;
CC Name=1C {ECO:0000269|PubMed:11906208}; Synonyms=G1c
CC {ECO:0000269|PubMed:10964959};
CC IsoId=Q8R4G0-3; Sequence=VSP_050549, VSP_050550;
CC Name=1D {ECO:0000269|PubMed:11906208}; Synonyms=G1d
CC {ECO:0000269|PubMed:10964959};
CC IsoId=Q8R4G0-4; Sequence=VSP_050551;
CC Name=1E {ECO:0000269|PubMed:11906208}; Synonyms=G1e
CC {ECO:0000269|PubMed:10964959};
CC IsoId=Q8R4G0-5; Sequence=VSP_050552, VSP_050553;
CC Name=1F {ECO:0000269|PubMed:11906208}; Synonyms=G1f
CC {ECO:0000269|PubMed:10964959};
CC IsoId=Q8R4G0-6; Sequence=VSP_050554, VSP_050555;
CC Name=1G {ECO:0000269|PubMed:11906208};
CC IsoId=Q8R4G0-7; Sequence=VSP_050558, VSP_050559;
CC Name=1H {ECO:0000269|PubMed:11906208};
CC IsoId=Q8R4G0-8; Sequence=VSP_050560, VSP_050561;
CC Name=1I {ECO:0000269|PubMed:11906208};
CC IsoId=Q8R4G0-9; Sequence=VSP_050556, VSP_050557;
CC Name=1J {ECO:0000269|PubMed:11906208};
CC IsoId=Q8R4G0-10; Sequence=VSP_050546;
CC -!- TISSUE SPECIFICITY: Expression is restricted primarily to neurons of
CC the CNS, particularly in the dorsal thalamus, olfactory bulb and
CC inferior colliculus. Isoform 1A and isoform 1D are the major products
CC in adult brain. {ECO:0000269|PubMed:10964959,
CC ECO:0000269|PubMed:11804778, ECO:0000269|PubMed:11906208}.
CC -!- DEVELOPMENTAL STAGE: Detected in the midbrain and the hindbrain regions
CC as early as 12 dpc. In the deep nucleus of the cerebellum, as well as
CC in the inferior colliculus and the thalamic regions, expression is
CC detected at 14 dpc, persists to postnatal day 1 and is down-regulated
CC by postnatal day 12. At 14 dpc, expression is segmented in dorsal
CC thalamus and pretectum in the midbrain and is regulated in a layer-
CC specific manner in the superior colliculus. In the olfactory bulb,
CC expression is detected at 14 dpc, increases by postnatal day 1 and is
CC maintained at a high level through postnatal day 21 and into adulthood.
CC {ECO:0000269|PubMed:10964959}.
CC -!- DOMAIN: The laminin N-terminal domain mediates 1:1 binding to NGL
CC ligand with sub-micromolar affinity. Three NGL-binding loops mediate
CC discrimination for LRRC4C/NGL1 among other NGLs by binding specifically
CC to its LRR repeats. This specificity drives the sorting of a mixed
CC population of molecules into discrete cell surface subdomains (By
CC similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10964959}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32353.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB038662; BAB12005.1; -; mRNA.
DR EMBL; AB038663; BAB12006.1; -; mRNA.
DR EMBL; AB038664; BAB12007.1; -; mRNA.
DR EMBL; AB038665; BAB12008.1; -; mRNA.
DR EMBL; AB038666; BAB12009.1; -; mRNA.
DR EMBL; AB038667; BAB12010.1; -; mRNA.
DR EMBL; AF475069; AAL84778.1; -; mRNA.
DR EMBL; AF475070; AAL84779.1; -; mRNA.
DR EMBL; AF475071; AAL84780.1; -; mRNA.
DR EMBL; AF475072; AAL84781.1; -; mRNA.
DR EMBL; AF475073; AAL84782.1; -; mRNA.
DR EMBL; AF475074; AAL84783.1; -; mRNA.
DR EMBL; AF475075; AAL84784.1; -; mRNA.
DR EMBL; AF475076; AAL84785.1; -; mRNA.
DR EMBL; AF475077; AAL84786.1; -; mRNA.
DR EMBL; AF475078; AAL84787.1; -; mRNA.
DR EMBL; AK034465; BAC28717.1; -; mRNA.
DR EMBL; AK173075; BAD32353.1; ALT_INIT; mRNA.
DR EMBL; BC079881; AAH79881.1; -; mRNA.
DR CCDS; CCDS38604.1; -. [Q8R4G0-1]
DR CCDS; CCDS59651.1; -. [Q8R4G0-3]
DR CCDS; CCDS59652.1; -. [Q8R4G0-2]
DR CCDS; CCDS59653.1; -. [Q8R4G0-5]
DR CCDS; CCDS59654.1; -. [Q8R4G0-4]
DR RefSeq; NP_001156820.1; NM_001163348.1. [Q8R4G0-2]
DR RefSeq; NP_001156821.1; NM_001163349.1. [Q8R4G0-3]
DR RefSeq; NP_001156822.1; NM_001163350.1. [Q8R4G0-4]
DR RefSeq; NP_001156823.1; NM_001163351.1.
DR RefSeq; NP_109624.1; NM_030699.2. [Q8R4G0-1]
DR RefSeq; NP_597995.1; NM_133488.1. [Q8R4G0-5]
DR RefSeq; XP_011238597.1; XM_011240295.2. [Q8R4G0-7]
DR AlphaFoldDB; Q8R4G0; -.
DR SMR; Q8R4G0; -.
DR BioGRID; 219827; 1.
DR IntAct; Q8R4G0; 1.
DR STRING; 10090.ENSMUSP00000072397; -.
DR GlyConnect; 2532; 2 N-Linked glycans (2 sites).
DR GlyGen; Q8R4G0; 4 sites, 2 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q8R4G0; -.
DR PaxDb; Q8R4G0; -.
DR PRIDE; Q8R4G0; -.
DR ProteomicsDB; 293758; -. [Q8R4G0-1]
DR ProteomicsDB; 293759; -. [Q8R4G0-2]
DR ProteomicsDB; 293760; -. [Q8R4G0-3]
DR ProteomicsDB; 293761; -. [Q8R4G0-4]
DR ProteomicsDB; 293762; -. [Q8R4G0-5]
DR ProteomicsDB; 293763; -. [Q8R4G0-6]
DR ProteomicsDB; 293764; -. [Q8R4G0-7]
DR ProteomicsDB; 293765; -. [Q8R4G0-8]
DR ProteomicsDB; 293766; -. [Q8R4G0-9]
DR ProteomicsDB; 293767; -. [Q8R4G0-10]
DR Antibodypedia; 33720; 167 antibodies from 29 providers.
DR DNASU; 80883; -.
DR Ensembl; ENSMUST00000072596; ENSMUSP00000072397; ENSMUSG00000059857. [Q8R4G0-1]
DR Ensembl; ENSMUST00000131027; ENSMUSP00000118800; ENSMUSG00000059857. [Q8R4G0-7]
DR Ensembl; ENSMUST00000133268; ENSMUSP00000117371; ENSMUSG00000059857. [Q8R4G0-3]
DR Ensembl; ENSMUST00000138344; ENSMUSP00000120688; ENSMUSG00000059857. [Q8R4G0-2]
DR Ensembl; ENSMUST00000138953; ENSMUSP00000116213; ENSMUSG00000059857. [Q8R4G0-4]
DR Ensembl; ENSMUST00000156177; ENSMUSP00000119534; ENSMUSG00000059857. [Q8R4G0-5]
DR GeneID; 80883; -.
DR KEGG; mmu:80883; -.
DR UCSC; uc008rai.2; mouse. [Q8R4G0-7]
DR UCSC; uc008raj.2; mouse. [Q8R4G0-2]
DR UCSC; uc008rak.2; mouse. [Q8R4G0-4]
DR UCSC; uc008ral.2; mouse. [Q8R4G0-1]
DR UCSC; uc008ram.2; mouse. [Q8R4G0-3]
DR UCSC; uc008rao.2; mouse. [Q8R4G0-5]
DR UCSC; uc008rap.1; mouse. [Q8R4G0-8]
DR UCSC; uc008raq.1; mouse. [Q8R4G0-9]
DR UCSC; uc008rar.2; mouse. [Q8R4G0-6]
DR CTD; 22854; -.
DR MGI; MGI:1934028; Ntng1.
DR VEuPathDB; HostDB:ENSMUSG00000059857; -.
DR eggNOG; KOG1836; Eukaryota.
DR eggNOG; KOG3512; Eukaryota.
DR GeneTree; ENSGT00940000153601; -.
DR HOGENOM; CLU_039838_1_1_1; -.
DR InParanoid; Q8R4G0; -.
DR OrthoDB; 117497at2759; -.
DR PhylomeDB; Q8R4G0; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 80883; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ntng1; mouse.
DR PRO; PR:Q8R4G0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R4G0; protein.
DR Bgee; ENSMUSG00000059857; Expressed in medial dorsal nucleus of thalamus and 156 other tissues.
DR ExpressionAtlas; Q8R4G0; baseline and differential.
DR Genevisible; Q8R4G0; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099029; C:anchored component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0150011; P:regulation of neuron projection arborization; IMP:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW Laminin EGF-like domain; Lipoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..510
FT /note="Netrin-G1"
FT /id="PRO_0000017093"
FT PROPEP 511..539
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000017094"
FT DOMAIN 46..296
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 297..356
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 364..419
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 420..469
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 80..91
FT /note="NGL discriminant loop I"
FT /evidence="ECO:0000250"
FT REGION 208..214
FT /note="NGL discriminant loop II"
FT /evidence="ECO:0000250"
FT REGION 273..275
FT /note="NGL discriminant loop III"
FT /evidence="ECO:0000250"
FT LIPID 510
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..50
FT /evidence="ECO:0000250"
FT DISULFID 72..92
FT /evidence="ECO:0000250"
FT DISULFID 80..88
FT /evidence="ECO:0000250"
FT DISULFID 182..206
FT /evidence="ECO:0000250"
FT DISULFID 297..306
FT /evidence="ECO:0000255"
FT DISULFID 299..315
FT /evidence="ECO:0000255"
FT DISULFID 317..326
FT /evidence="ECO:0000255"
FT DISULFID 329..354
FT /evidence="ECO:0000255"
FT DISULFID 364..373
FT /evidence="ECO:0000255"
FT DISULFID 366..384
FT /evidence="ECO:0000255"
FT DISULFID 387..396
FT /evidence="ECO:0000255"
FT DISULFID 399..417
FT /evidence="ECO:0000255"
FT DISULFID 420..432
FT /evidence="ECO:0000255"
FT DISULFID 422..438
FT /evidence="ECO:0000255"
FT DISULFID 440..449
FT /evidence="ECO:0000255"
FT DISULFID 452..462
FT /evidence="ECO:0000255"
FT DISULFID 488..497
FT /evidence="ECO:0000250"
FT VAR_SEQ 297..539
FT /note="Missing (in isoform 1J)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050546"
FT VAR_SEQ 363..464
FT /note="NCECFGHSNRCSYIDLLNTVICVSCKHNTRGQHCELCRLGYFRNASAQLDDE
FT NVCIECYCNPLGSIHDRCNGSGFCECKTGTTGPKCDECLPGNSWYYGCQP -> TPPKF
FT NRIWPNISSLEVSNPKQVAPKLALSTVSSVQVANHKRA (in isoform 1D)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208"
FT /id="VSP_050551"
FT VAR_SEQ 363..463
FT /note="Missing (in isoform 1C)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208, ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050549"
FT VAR_SEQ 363..418
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208"
FT /id="VSP_050547"
FT VAR_SEQ 363..388
FT /note="NCECFGHSNRCSYIDLLNTVICVSCK -> TPPKFNRIWPNISSLEVSNPKQ
FT GRSI (in isoform 1I)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050556"
FT VAR_SEQ 363..385
FT /note="NCECFGHSNRCSYIDLLNTVICV -> TPPKFNRIWPNISSLEVSNPKQA
FT (in isoform 1E)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208, ECO:0000303|PubMed:16141072"
FT /id="VSP_050552"
FT VAR_SEQ 363..364
FT /note="NC -> SK (in isoform 1F)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208"
FT /id="VSP_050554"
FT VAR_SEQ 365..539
FT /note="Missing (in isoform 1F)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208"
FT /id="VSP_050555"
FT VAR_SEQ 386..464
FT /note="Missing (in isoform 1E)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208, ECO:0000303|PubMed:16141072"
FT /id="VSP_050553"
FT VAR_SEQ 389..539
FT /note="Missing (in isoform 1I)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050557"
FT VAR_SEQ 419..463
FT /note="Missing (in isoform 1G)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050558"
FT VAR_SEQ 419..438
FT /note="ECYCNPLGSIHDRCNGSGFC -> GQFHYDFSFCSVPLELWGAG (in
FT isoform 1H)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050560"
FT VAR_SEQ 419
FT /note="E -> K (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208"
FT /id="VSP_050548"
FT VAR_SEQ 439..539
FT /note="Missing (in isoform 1H)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050561"
FT VAR_SEQ 464
FT /note="P -> T (in isoform 1C)"
FT /evidence="ECO:0000303|PubMed:10964959,
FT ECO:0000303|PubMed:11906208, ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050550"
FT VAR_SEQ 464
FT /note="P -> A (in isoform 1G)"
FT /evidence="ECO:0000303|PubMed:11906208"
FT /id="VSP_050559"
FT CONFLICT 166
FT /note="L -> F (in Ref. 2; AAL84778/AAL84780/AAL84781/
FT AAL84782/AAL84784/AAL84785/AAL84786/AAL84787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 60566 MW; DDC9BA2C577B29D5 CRC64;
MYLSRFLSIH ALWVTVSSVM QPYLFVWGHY DVCKSLIYTE EGKVWDYTAC QPESTDMTKY
LKVKLDPPDI TCGDPPESFC AMGNPYMCNN ECDASTPELA HPPELMFDFE GRHPSTFWQS
ATWKEYPKPL QVNITLSWSK TIELTDNIVI TFESGRPDQM ILEKSLDYGR TWQPYQYYAT
DCLHAFHMDP KSVKDLSQHT VLEIICTEEY STGYSTNSKI IHFEIKDRFA FFAGPRLRNM
ASLYGQLDTT KKLRDFFTVT DLRIRLLRPA VGEIFVDELH LARYFYAISD IKVRGRCKCN
LHATSCLYDN SKLTCECEHN TTGPDCGKCK KNYQGRPWSP GSYLPIPKGT ANTCIPSISS
IGNCECFGHS NRCSYIDLLN TVICVSCKHN TRGQHCELCR LGYFRNASAQ LDDENVCIEC
YCNPLGSIHD RCNGSGFCEC KTGTTGPKCD ECLPGNSWYY GCQPNVCDNE LLHCQNGGTC
QNNVRCACPD AYTGILCEKL RCEEAGSCGS ESGQGAPPRG SPALLLLTML LGTAGPLVF
