CR1L_MOUSE
ID CR1L_MOUSE Reviewed; 483 AA.
AC Q64735; E9QL18; Q3TV30; Q58E68; Q61447; Q61449; Q8CF59; Q8K328;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Complement component receptor 1-like protein;
DE AltName: Full=Complement regulatory protein Crry;
DE AltName: Full=Protein p65;
DE Flags: Precursor;
GN Name=Cr1l; Synonyms=Crry, Cry;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RC STRAIN=BALB/cJ;
RX PubMed=2307848;
RA Paul M.S., Aegerter-Shaw M., Cepek K., Miller M.D., Weis J.H.;
RT "The murine complement receptor gene family: III. The genomic and
RT transcriptional complexity of the Crry and Crry-ps genes.";
RL J. Immunol. 144:1988-1996(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 64-437 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-477 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 12-167 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver, and Spleen;
RX PubMed=2911011;
RA Paul M.S., Aegerter-Shaw M., O'Brien S.E., Kurtz C.B., Weis J.H.;
RT "The murine complement receptor gene family analysis of mCRY gene products
RT and their homology to human CR1.";
RL J. Immunol. 142:582-589(1989).
RN [6]
RP FUNCTION.
RX PubMed=1730912; DOI=10.1084/jem.175.1.121;
RA Molina H., Wong W., Kinoshita T., Brenner C., Foley S., Holers V.M.;
RT "Distinct receptor and regulatory properties of recombinant mouse
RT complement receptor 1 (CR1) and Crry, the two genetic homologues of human
RT CR1.";
RL J. Exp. Med. 175:121-129(1992).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=7691944;
RA Li B., Sallee C., Dehoff M., Foley S., Molina H., Holers V.M.;
RT "Mouse Crry/p65. Characterization of monoclonal antibodies and the tissue
RT distribution of a functional homologue of human MCP and DAF.";
RL J. Immunol. 151:4295-4305(1993).
RN [8]
RP FUNCTION.
RX PubMed=7528766; DOI=10.1084/jem.181.1.151;
RA Kim Y.-U., Kinoshita T., Molina H., Hourcade D., Seya T., Wagner L.M.,
RA Holers V.M.;
RT "Mouse complement regulatory protein Crry/p65 uses the specific mechanisms
RT of both human decay-accelerating factor and membrane cofactor protein.";
RL J. Exp. Med. 181:151-159(1995).
RN [9]
RP FUNCTION.
RX PubMed=10779754; DOI=10.4049/jimmunol.164.9.4533;
RA Fernandez-Centeno E., de Ojeda G., Rojo J.M., Portoles P.;
RT "Crry/p65, a membrane complement regulatory protein, has costimulatory
RT properties on mouse T cells.";
RL J. Immunol. 164:4533-4542(2000).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10642554; DOI=10.1126/science.287.5452.498;
RA Xu C., Mao D., Holers V.M., Palanca B., Cheng A.M., Molina H.;
RT "A critical role for murine complement regulator crry in fetomaternal
RT tolerance.";
RL Science 287:498-501(2000).
RN [11]
RP FUNCTION.
RX PubMed=11986227; DOI=10.1182/blood.v99.10.3707;
RA Miwa T., Zhou L., Hilliard B., Molina H., Song W.-C.;
RT "Crry, but not CD59 and DAF, is indispensable for murine erythrocyte
RT protection in vivo from spontaneous complement attack.";
RL Blood 99:3707-3716(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; THR-463 AND SER-477, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; SER-460; SER-468 AND
RP SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, and Spleen;
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 [15]
RP 3D-STRUCTURE MODELING OF 84-401.
RX PubMed=12767833; DOI=10.1016/s0022-2836(03)00492-3;
RA Aslam M., Guthridge J.M., Hack B.K., Quigg R.J., Holers V.M., Perkins S.J.;
RT "The extended multidomain solution structures of the complement protein
RT Crry and its chimeric conjugate Crry-Ig by scattering, analytical
RT ultracentrifugation and constrained modelling: implications for function
RT and therapy.";
RL J. Mol. Biol. 329:525-550(2003).
CC -!- FUNCTION: Acts as a cofactor for complement factor I, a serine protease
CC which protects autologous cells against complement-mediated injury by
CC cleaving C3b and C4b deposited on host tissue. Also acts as a decay-
CC accelerating factor, preventing the formation of C4b2a and C3bBb, the
CC amplification convertases of the complement cascade. Plays a crucial
CC role in early embryonic development by maintaining fetomaternal
CC tolerance. Also acts as a costimulatory factor for T-cells which favors
CC IL-4 secretion. {ECO:0000269|PubMed:10642554,
CC ECO:0000269|PubMed:10779754, ECO:0000269|PubMed:11986227,
CC ECO:0000269|PubMed:1730912, ECO:0000269|PubMed:7528766}.
CC -!- SUBUNIT: Interacts with C3b. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64735-2; Sequence=VSP_019050;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC {ECO:0000269|PubMed:2911011, ECO:0000269|PubMed:7691944}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in trophoblasts at 7.5 dpc, and
CC in the maternally derived decidual tissues until 16 dpc. Expressed only
CC at low levels in the embryo itself. {ECO:0000269|PubMed:10642554}.
CC -!- DISRUPTION PHENOTYPE: Death between 9.5 and 13.5 dpc from developmental
CC arrest. {ECO:0000269|PubMed:10642554}.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37477.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC25098.1; 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; M34173; AAA37467.1; -; Genomic_DNA.
DR EMBL; M34164; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34165; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34166; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34167; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34168; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34169; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34170; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34171; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34172; AAA37467.1; JOINED; Genomic_DNA.
DR EMBL; M34173; AAA37468.1; -; Genomic_DNA.
DR EMBL; M34164; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34165; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34166; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34167; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34168; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34169; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34170; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34171; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; M34172; AAA37468.1; JOINED; Genomic_DNA.
DR EMBL; AK004825; BAC25098.1; ALT_FRAME; mRNA.
DR EMBL; AK160440; BAE35790.1; -; mRNA.
DR EMBL; AC139206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028945; AAH28945.1; -; mRNA.
DR EMBL; BC092048; AAH92048.1; -; mRNA.
DR EMBL; M23529; AAA37477.1; ALT_FRAME; mRNA.
DR EMBL; M23446; AAA37478.1; -; mRNA.
DR CCDS; CCDS15641.1; -. [Q64735-2]
DR PIR; A43519; A43519.
DR PIR; B30550; B30550.
DR PIR; I55975; I55975.
DR RefSeq; NP_038527.2; NM_013499.2. [Q64735-2]
DR PDB; 1NTL; X-ray; 30.00 A; A/B=83-401.
DR PDBsum; 1NTL; -.
DR AlphaFoldDB; Q64735; -.
DR SMR; Q64735; -.
DR BioGRID; 198901; 2.
DR STRING; 10090.ENSMUSP00000074902; -.
DR GlyGen; Q64735; 2 sites.
DR iPTMnet; Q64735; -.
DR PhosphoSitePlus; Q64735; -.
DR EPD; Q64735; -.
DR jPOST; Q64735; -.
DR MaxQB; Q64735; -.
DR PeptideAtlas; Q64735; -.
DR PRIDE; Q64735; -.
DR ProteomicsDB; 285296; -. [Q64735-1]
DR ProteomicsDB; 285297; -. [Q64735-2]
DR ABCD; Q64735; 22 sequenced antibodies.
DR Antibodypedia; 4269; 1260 antibodies from 45 providers.
DR DNASU; 12946; -.
DR Ensembl; ENSMUST00000075451; ENSMUSP00000074902; ENSMUSG00000016481. [Q64735-2]
DR GeneID; 12946; -.
DR KEGG; mmu:12946; -.
DR UCSC; uc007eeu.1; mouse. [Q64735-1]
DR UCSC; uc007eev.1; mouse. [Q64735-2]
DR CTD; 1379; -.
DR MGI; MGI:88513; Cr1l.
DR VEuPathDB; HostDB:ENSMUSG00000016481; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000160375; -.
DR InParanoid; Q64735; -.
DR OMA; AAFWIFK; -.
DR OrthoDB; 46968at2759; -.
DR PhylomeDB; Q64735; -.
DR TreeFam; TF334137; -.
DR BioGRID-ORCS; 12946; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Cr1l; mouse.
DR EvolutionaryTrace; Q64735; -.
DR PRO; PR:Q64735; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q64735; protein.
DR Bgee; ENSMUSG00000016481; Expressed in aortic valve and 251 other tissues.
DR ExpressionAtlas; Q64735; baseline and differential.
DR Genevisible; Q64735; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0001851; F:complement component C3b binding; ISO:MGI.
DR GO; GO:0004877; F:complement component C3b receptor activity; ISO:MGI.
DR GO; GO:0001855; F:complement component C4b binding; ISO:MGI.
DR GO; GO:0001861; F:complement component C4b receptor activity; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR GO; GO:0006956; P:complement activation; IMP:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045916; P:negative regulation of complement activation; IMP:MGI.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0030449; P:regulation of complement activation; IMP:MGI.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0002456; P:T cell mediated immunity; IBA:GO_Central.
DR CDD; cd00033; CCP; 5.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS50923; SUSHI; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complement pathway;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Phosphoprotein; Pregnancy; Receptor;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..483
FT /note="Complement component receptor 1-like protein"
FT /id="PRO_0000238978"
FT TOPO_DOM 41..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 83..143
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 144..205
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 206..276
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 278..338
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 340..400
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 115..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 146..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 173..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 208..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 237..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 280..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 309..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 342..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 371..398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 40..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2911011"
FT /id="VSP_019050"
FT CONFLICT 21
FT /note="G -> A (in Ref. 5; AAA37477)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="E -> A (in Ref. 4; AAH92048)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..67
FT /note="ADSK -> GRLQ (in Ref. 2; BAE35790)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="Missing (in Ref. 3; AC139206)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="L -> M (in Ref. 4; AAH92048)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> E (in Ref. 5; AAA37477)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> P (in Ref. 4; AAH92048)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="D -> N (in Ref. 4; AAH92048)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..437
FT /note="NTT -> TRF (in Ref. 2; BAE35790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 53763 MW; 259BFFED4CE547C1 CRC64;
MEVSSRSSEP LDPVWLLVAF GRGGVKLEVL LLFLLPFTLG ELRGGLGKHG HTVHREPAVN
RLCADSKRWS GLPVSAQRPF PMGHCPAPSQ LPSAKPINLT DESMFPIGTY LLYECLPGYI
KRQFSITCKQ DSTWTSAEDK CIRKQCKTPS DPENGLVHVH TGIQFGSRIN YTCNQGYRLI
GSSSAVCVIT DQSVDWDTEA PICEWIPCEI PPGIPNGDFF SSTREDFHYG MVVTYRCNTD
ARGKALFNLV GEPSLYCTSN DGEIGVWSGP PPQCIELNKC TPPPYVENAV MLSENRSLFS
LRDIVEFRCH PGFIMKGASS VHCQSLNKWE PELPSCFKGV ICRLPQEMSG FQKGLGMKKE
YYYGENVTLE CEDGYTLEGS SQSQCQSDGS WNPLLAKCVS RSISGLIVGI FIGIIVFILV
IIVFIWMILK YKKRNTTDEK YKEVGIHLNY KEDSCVRLQS LLTSQENSST TSPARNSLTQ
EVS
