Full text data of MICALL2
MICALL2
(JRAB)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
MICAL-like protein 2 (Junctional Rab13-binding protein; Molecule interacting with CasL-like 2; MICAL-L2)
MICAL-like protein 2 (Junctional Rab13-binding protein; Molecule interacting with CasL-like 2; MICAL-L2)
UniProt
Q8IY33
ID MILK2_HUMAN Reviewed; 904 AA.
AC Q8IY33; D3YTD2; Q7RTP4; Q7Z655; Q8TEQ4; Q9H5F9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2003, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=MICAL-like protein 2;
DE AltName: Full=Junctional Rab13-binding protein;
DE AltName: Full=Molecule interacting with CasL-like 2;
DE Short=MICAL-L2;
GN Name=MICALL2; Synonyms=JRAB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Brain cortex, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION.
RX PubMed=12110185; DOI=10.1016/S0092-8674(02)00794-8;
RA Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.;
RT "MICALs, a family of conserved flavoprotein oxidoreductases, function
RT in plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
RN [8]
RP INTERACTION WITH RAB13.
RX PubMed=16525024; DOI=10.1091/mbc.E05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-649; SER-658
RP AND SER-660, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INTERACTION WITH FLNA.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K.,
RA Kitamura T., Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
CC -!- FUNCTION: Effector of small Rab GTPases which is involved in
CC junctional complexes assembly through the regulation of cell
CC adhesion molecules transport to the plasma membrane and actin
CC cytoskeleton reorganization. Regulates the endocytic recycling of
CC occludins, claudins and E-cadherin to the plasma membrane and may
CC thereby regulate the establishment of tight junctions and adherens
CC junctions. In parallel, may regulate actin cytoskeleton
CC reorganization directly through interaction with F-actin or
CC indirectly through actinins and filamins. Most probably involved
CC in the processes of epithelial cell differentiation, cell
CC spreading and neurite outgrowth (By similarity).
CC -!- SUBUNIT: Interacts with RAB13 (GTP-bound form); competes with
CC RAB8A and is involved in tight junctions assembly. Interacts with
CC RAB8A; competes with RAB13 and is involved in E-cadherin endocytic
CC recycling (By similarity). Interacts with RAB8B (By similarity).
CC Interacts (preferentially in opened conformation) with ACTN1 and
CC ACTN4; stimulated by RAB13 activation (By similarity). Interacts
CC (via CH domain) with the filamins FLNA, FLNB and FLNC (via actin-
CC binding domain).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC (By similarity). Cell junction, tight junction (By similarity).
CC Recycling endosome (By similarity). Cell projection (By
CC similarity). Cytoplasm, cytoskeleton (By similarity). Cytoplasm,
CC cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IY33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY33-2; Sequence=VSP_009854, VSP_009855;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8IY33-3; Sequence=VSP_009856;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q8IY33-4; Sequence=VSP_009857;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q8IY33-5; Sequence=VSP_009858;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: Probably exists in a closed and an opened conformation due
CC to interaction of the C-terminal coiled-coil domain with an N-
CC terminal region including the CH (calponin-homology) and the LIM
CC zinc-binding domain. The conformational change is regulated by
CC RAB13 (By similarity).
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15667.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB84894.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AL833704; CAD98087.1; -; mRNA.
DR EMBL; AK027124; BAB15667.1; ALT_INIT; mRNA.
DR EMBL; AK126808; BAC86702.1; -; mRNA.
DR EMBL; AK074068; BAB84894.1; ALT_INIT; mRNA.
DR EMBL; AC102953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87200.1; -; Genomic_DNA.
DR EMBL; BC037988; AAH37988.1; -; mRNA.
DR EMBL; BK000467; DAA01346.1; -; mRNA.
DR RefSeq; NP_891554.1; NM_182924.3.
DR UniGene; Hs.376617; -.
DR UniGene; Hs.663699; -.
DR ProteinModelPortal; Q8IY33; -.
DR SMR; Q8IY33; 6-106, 167-248.
DR IntAct; Q8IY33; 2.
DR STRING; 9606.ENSP00000297508; -.
DR PhosphoSite; Q8IY33; -.
DR DMDM; 46396456; -.
DR PaxDb; Q8IY33; -.
DR PRIDE; Q8IY33; -.
DR DNASU; 79778; -.
DR Ensembl; ENST00000297508; ENSP00000297508; ENSG00000164877.
DR Ensembl; ENST00000405088; ENSP00000385928; ENSG00000164877.
DR Ensembl; ENST00000413446; ENSP00000405415; ENSG00000164877.
DR GeneID; 79778; -.
DR KEGG; hsa:79778; -.
DR UCSC; uc003ski.4; human.
DR CTD; 79778; -.
DR GeneCards; GC07M001441; -.
DR HGNC; HGNC:29672; MICALL2.
DR HPA; HPA025695; -.
DR neXtProt; NX_Q8IY33; -.
DR PharmGKB; PA162395928; -.
DR eggNOG; COG5069; -.
DR HOGENOM; HOG000290690; -.
DR HOVERGEN; HBG052476; -.
DR InParanoid; Q8IY33; -.
DR OMA; IRALQQW; -.
DR OrthoDB; EOG7JT6VM; -.
DR PhylomeDB; Q8IY33; -.
DR ChiTaRS; MICALL2; human.
DR GenomeRNAi; 79778; -.
DR NextBio; 35491156; -.
DR PRO; PR:Q8IY33; -.
DR ArrayExpress; Q8IY33; -.
DR Bgee; Q8IY33; -.
DR CleanEx; HS_MICALL2; -.
DR Genevestigator; Q8IY33; -.
DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005923; C:tight junction; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0070830; P:tight junction assembly; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 2.10.110.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR022735; DUF3585.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Endosome;
KW LIM domain; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome; Tight junction; Zinc.
FT CHAIN 1 904 MICAL-like protein 2.
FT /FTId=PRO_0000075850.
FT DOMAIN 1 104 CH.
FT DOMAIN 186 248 LIM zinc-binding.
FT REGION 1 260 Forms an intramolecular interaction with
FT the C-terminal coiled coil domain keeping
FT the protein in a closed conformation (By
FT similarity).
FT REGION 261 697 Mediates targeting to the cell plasma
FT membrane (By similarity).
FT REGION 261 388 Necessary and sufficient for interaction
FT with actinins (By similarity).
FT REGION 698 807 Forms an intramolecular interaction with
FT the N-terminal CH and LIM zinc-binding
FT domains-containing region keeping the
FT protein in a closed conformation (By
FT similarity).
FT REGION 807 903 Mediates interaction with RAB13 and is
FT required for transition from the closed
FT to the opened conformation (By
FT similarity).
FT COILED 735 771 Potential.
FT COMPBIAS 356 359 Poly-Ala.
FT COMPBIAS 392 397 Poly-Ser.
FT COMPBIAS 663 666 Poly-Arg.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 494 494 Phosphoserine.
FT MOD_RES 649 649 Phosphoserine.
FT MOD_RES 658 658 Phosphoserine.
FT MOD_RES 660 660 Phosphoserine.
FT MOD_RES 726 726 Phosphoserine (By similarity).
FT VAR_SEQ 1 570 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILH
FT RHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAE
FT DMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMAGVKRASE
FT DSEEEPSGKKAPVQAAKLPSPAPARKPPLSPAQTNPVVQRR
FT NEGAGGPPPKTDQALAGSLVSSTCGVCGKHVHLVQRHLADG
FT RLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSHLPAAA
FT SASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAW
FT EPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLA
FT PTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAP
FT DPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSA
FT SRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQ
FT ARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQ
FT ASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALPP
FT AGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQ ->
FT MALSSWAQGTSWAAKGFSRSFSLAEFSLLKPRAGSCRTQEP
FT RKPADGQPWLRCSPCTGGQRIWVHGAHPATSPPIRQKGKLR
FT PRGRESFPQGHTAQESQLGAPPLTPCPVLLMPPGRLAVGVS
FT EGGVAMGRWQGEAQPPLQTPHSQHSFLTPRPLASHP (in
FT isoform 3).
FT /FTId=VSP_009856.
FT VAR_SEQ 1 48 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILH
FT RHRPDLI -> MFLSSR (in isoform 2).
FT /FTId=VSP_009854.
FT VAR_SEQ 29 240 Missing (in isoform 5).
FT /FTId=VSP_009858.
FT VAR_SEQ 571 904 DMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRA
FT LAEPRAGEAPRKVSGSFAGSVHITLTPVRPDRTPRPASPGP
FT SLPARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQS
FT WKEEEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDY
FT LSPEEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAED
FT SLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEG
FT ELRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDS
FT LDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKS
FT KSSPSQ -> GE (in isoform 4).
FT /FTId=VSP_009857.
FT VAR_SEQ 656 904 ARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQSWKE
FT EEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDYLSP
FT EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLM
FT VDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELR
FT RLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDE
FT DRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKSKSS
FT PSQ -> GPPPHPAAGDWPSLPASTFVTTGFGRSPLARKPE
FT CRAGRRRRRNLTFRANQGDPCPRPMSLLCLARR (in
FT isoform 2).
FT /FTId=VSP_009855.
FT VARIANT 480 480 A -> P (in dbSNP:rs12540098).
FT /FTId=VAR_034071.
FT VARIANT 519 519 P -> L (in dbSNP:rs4075307).
FT /FTId=VAR_034072.
FT VARIANT 623 623 K -> R (in dbSNP:rs61287564).
FT /FTId=VAR_061356.
FT VARIANT 711 711 L -> V (in dbSNP:rs11980797).
FT /FTId=VAR_050159.
FT CONFLICT 255 255 L -> M (in Ref. 1; CAD98087).
FT CONFLICT 285 285 S -> L (in Ref. 2; BAB15667).
FT CONFLICT 706 706 K -> R (in Ref. 2; BAB15667).
SQ SEQUENCE 904 AA; 97502 MW; A2C360EDDEFFA2EF CRC64;
MAAIRALQQW CRQQCEGYRD VNICNMTTSF RDGLAFCAIL HRHRPDLINF SALKKENIYE
NNKLAFRVAE EHLGIPALLD AEDMVALKVP DRLSILTYVS QYYNYFHGRS PIGGMAGVKR
ASEDSEEEPS GKKAPVQAAK LPSPAPARKP PLSPAQTNPV VQRRNEGAGG PPPKTDQALA
GSLVSSTCGV CGKHVHLVQR HLADGRLYHR SCFRCKQCSC TLHSGAYKAT GEPGTFVCTS
HLPAAASASP KLTGLVPRQP GAMGVDSRTS CSPQKAQEAN KARPSAWEPA AGNSPARASV
PAAPNPAATS ATSVHVRSPA RPSESRLAPT PTEGKVRPRV TNSSPMGWSS AAPCTAAAAS
HPAVPPSAPD PRPATPQGGG APRVAAPQTT LSSSSTSAAT VDPPAWTPSA SRTQQARNKF
FQTSAVPPGT SLSGRGPTPS LVLSKDSSKE QARNFLKQAL SALEEAGAPA PGRPSPATAA
VPSSQPKTEA PQASPLAKPL QSSSPRVLGL PSRMEPPAPL STSSTSQASA LPPAGRRNLA
ESSGVGRVGA GSRPKPEAPM AKGKSTTLTQ DMSTSLQEGQ EDGPAGWRAN LKPVDRRSPA
ERTLKPKEPR ALAEPRAGEA PRKVSGSFAG SVHITLTPVR PDRTPRPASP GPSLPARSPS
PPRRRRLAVP ASLDVCDNWL RPEPPGQEAR VQSWKEEEKK PHLQGKPGRP LSPANVPALP
GETVTSPVRL HPDYLSPEEI QRQLQDIERR LDALELRGVE LEKRLRAAEG DDAEDSLMVD
WFWLIHEKQL LLRQESELMY KSKAQRLEEQ QLDIEGELRR LMAKPEALKS LQERRREQEL
LEQYVSTVND RSDIVDSLDE DRLREQEEDQ MLRDMIEKLG LQRKKSKFRL SKIWSPKSKS
SPSQ
//
ID MILK2_HUMAN Reviewed; 904 AA.
AC Q8IY33; D3YTD2; Q7RTP4; Q7Z655; Q8TEQ4; Q9H5F9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2003, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=MICAL-like protein 2;
DE AltName: Full=Junctional Rab13-binding protein;
DE AltName: Full=Molecule interacting with CasL-like 2;
DE Short=MICAL-L2;
GN Name=MICALL2; Synonyms=JRAB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Brain cortex, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION.
RX PubMed=12110185; DOI=10.1016/S0092-8674(02)00794-8;
RA Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.;
RT "MICALs, a family of conserved flavoprotein oxidoreductases, function
RT in plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
RN [8]
RP INTERACTION WITH RAB13.
RX PubMed=16525024; DOI=10.1091/mbc.E05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-649; SER-658
RP AND SER-660, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INTERACTION WITH FLNA.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K.,
RA Kitamura T., Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
CC -!- FUNCTION: Effector of small Rab GTPases which is involved in
CC junctional complexes assembly through the regulation of cell
CC adhesion molecules transport to the plasma membrane and actin
CC cytoskeleton reorganization. Regulates the endocytic recycling of
CC occludins, claudins and E-cadherin to the plasma membrane and may
CC thereby regulate the establishment of tight junctions and adherens
CC junctions. In parallel, may regulate actin cytoskeleton
CC reorganization directly through interaction with F-actin or
CC indirectly through actinins and filamins. Most probably involved
CC in the processes of epithelial cell differentiation, cell
CC spreading and neurite outgrowth (By similarity).
CC -!- SUBUNIT: Interacts with RAB13 (GTP-bound form); competes with
CC RAB8A and is involved in tight junctions assembly. Interacts with
CC RAB8A; competes with RAB13 and is involved in E-cadherin endocytic
CC recycling (By similarity). Interacts with RAB8B (By similarity).
CC Interacts (preferentially in opened conformation) with ACTN1 and
CC ACTN4; stimulated by RAB13 activation (By similarity). Interacts
CC (via CH domain) with the filamins FLNA, FLNB and FLNC (via actin-
CC binding domain).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC (By similarity). Cell junction, tight junction (By similarity).
CC Recycling endosome (By similarity). Cell projection (By
CC similarity). Cytoplasm, cytoskeleton (By similarity). Cytoplasm,
CC cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IY33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY33-2; Sequence=VSP_009854, VSP_009855;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8IY33-3; Sequence=VSP_009856;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q8IY33-4; Sequence=VSP_009857;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q8IY33-5; Sequence=VSP_009858;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: Probably exists in a closed and an opened conformation due
CC to interaction of the C-terminal coiled-coil domain with an N-
CC terminal region including the CH (calponin-homology) and the LIM
CC zinc-binding domain. The conformational change is regulated by
CC RAB13 (By similarity).
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15667.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB84894.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AL833704; CAD98087.1; -; mRNA.
DR EMBL; AK027124; BAB15667.1; ALT_INIT; mRNA.
DR EMBL; AK126808; BAC86702.1; -; mRNA.
DR EMBL; AK074068; BAB84894.1; ALT_INIT; mRNA.
DR EMBL; AC102953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87200.1; -; Genomic_DNA.
DR EMBL; BC037988; AAH37988.1; -; mRNA.
DR EMBL; BK000467; DAA01346.1; -; mRNA.
DR RefSeq; NP_891554.1; NM_182924.3.
DR UniGene; Hs.376617; -.
DR UniGene; Hs.663699; -.
DR ProteinModelPortal; Q8IY33; -.
DR SMR; Q8IY33; 6-106, 167-248.
DR IntAct; Q8IY33; 2.
DR STRING; 9606.ENSP00000297508; -.
DR PhosphoSite; Q8IY33; -.
DR DMDM; 46396456; -.
DR PaxDb; Q8IY33; -.
DR PRIDE; Q8IY33; -.
DR DNASU; 79778; -.
DR Ensembl; ENST00000297508; ENSP00000297508; ENSG00000164877.
DR Ensembl; ENST00000405088; ENSP00000385928; ENSG00000164877.
DR Ensembl; ENST00000413446; ENSP00000405415; ENSG00000164877.
DR GeneID; 79778; -.
DR KEGG; hsa:79778; -.
DR UCSC; uc003ski.4; human.
DR CTD; 79778; -.
DR GeneCards; GC07M001441; -.
DR HGNC; HGNC:29672; MICALL2.
DR HPA; HPA025695; -.
DR neXtProt; NX_Q8IY33; -.
DR PharmGKB; PA162395928; -.
DR eggNOG; COG5069; -.
DR HOGENOM; HOG000290690; -.
DR HOVERGEN; HBG052476; -.
DR InParanoid; Q8IY33; -.
DR OMA; IRALQQW; -.
DR OrthoDB; EOG7JT6VM; -.
DR PhylomeDB; Q8IY33; -.
DR ChiTaRS; MICALL2; human.
DR GenomeRNAi; 79778; -.
DR NextBio; 35491156; -.
DR PRO; PR:Q8IY33; -.
DR ArrayExpress; Q8IY33; -.
DR Bgee; Q8IY33; -.
DR CleanEx; HS_MICALL2; -.
DR Genevestigator; Q8IY33; -.
DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0005923; C:tight junction; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0070830; P:tight junction assembly; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 2.10.110.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR022735; DUF3585.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Endosome;
KW LIM domain; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome; Tight junction; Zinc.
FT CHAIN 1 904 MICAL-like protein 2.
FT /FTId=PRO_0000075850.
FT DOMAIN 1 104 CH.
FT DOMAIN 186 248 LIM zinc-binding.
FT REGION 1 260 Forms an intramolecular interaction with
FT the C-terminal coiled coil domain keeping
FT the protein in a closed conformation (By
FT similarity).
FT REGION 261 697 Mediates targeting to the cell plasma
FT membrane (By similarity).
FT REGION 261 388 Necessary and sufficient for interaction
FT with actinins (By similarity).
FT REGION 698 807 Forms an intramolecular interaction with
FT the N-terminal CH and LIM zinc-binding
FT domains-containing region keeping the
FT protein in a closed conformation (By
FT similarity).
FT REGION 807 903 Mediates interaction with RAB13 and is
FT required for transition from the closed
FT to the opened conformation (By
FT similarity).
FT COILED 735 771 Potential.
FT COMPBIAS 356 359 Poly-Ala.
FT COMPBIAS 392 397 Poly-Ser.
FT COMPBIAS 663 666 Poly-Arg.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 494 494 Phosphoserine.
FT MOD_RES 649 649 Phosphoserine.
FT MOD_RES 658 658 Phosphoserine.
FT MOD_RES 660 660 Phosphoserine.
FT MOD_RES 726 726 Phosphoserine (By similarity).
FT VAR_SEQ 1 570 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILH
FT RHRPDLINFSALKKENIYENNKLAFRVAEEHLGIPALLDAE
FT DMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMAGVKRASE
FT DSEEEPSGKKAPVQAAKLPSPAPARKPPLSPAQTNPVVQRR
FT NEGAGGPPPKTDQALAGSLVSSTCGVCGKHVHLVQRHLADG
FT RLYHRSCFRCKQCSCTLHSGAYKATGEPGTFVCTSHLPAAA
FT SASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAW
FT EPAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLA
FT PTPTEGKVRPRVTNSSPMGWSSAAPCTAAAASHPAVPPSAP
FT DPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAWTPSA
FT SRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQ
FT ARNFLKQALSALEEAGAPAPGRPSPATAAVPSSQPKTEAPQ
FT ASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSSTSQASALPP
FT AGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQ ->
FT MALSSWAQGTSWAAKGFSRSFSLAEFSLLKPRAGSCRTQEP
FT RKPADGQPWLRCSPCTGGQRIWVHGAHPATSPPIRQKGKLR
FT PRGRESFPQGHTAQESQLGAPPLTPCPVLLMPPGRLAVGVS
FT EGGVAMGRWQGEAQPPLQTPHSQHSFLTPRPLASHP (in
FT isoform 3).
FT /FTId=VSP_009856.
FT VAR_SEQ 1 48 MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILH
FT RHRPDLI -> MFLSSR (in isoform 2).
FT /FTId=VSP_009854.
FT VAR_SEQ 29 240 Missing (in isoform 5).
FT /FTId=VSP_009858.
FT VAR_SEQ 571 904 DMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRA
FT LAEPRAGEAPRKVSGSFAGSVHITLTPVRPDRTPRPASPGP
FT SLPARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQS
FT WKEEEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDY
FT LSPEEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAED
FT SLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEG
FT ELRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDS
FT LDEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKS
FT KSSPSQ -> GE (in isoform 4).
FT /FTId=VSP_009857.
FT VAR_SEQ 656 904 ARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQSWKE
FT EEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDYLSP
FT EEIQRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLM
FT VDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELR
FT RLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSLDE
FT DRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKSKSS
FT PSQ -> GPPPHPAAGDWPSLPASTFVTTGFGRSPLARKPE
FT CRAGRRRRRNLTFRANQGDPCPRPMSLLCLARR (in
FT isoform 2).
FT /FTId=VSP_009855.
FT VARIANT 480 480 A -> P (in dbSNP:rs12540098).
FT /FTId=VAR_034071.
FT VARIANT 519 519 P -> L (in dbSNP:rs4075307).
FT /FTId=VAR_034072.
FT VARIANT 623 623 K -> R (in dbSNP:rs61287564).
FT /FTId=VAR_061356.
FT VARIANT 711 711 L -> V (in dbSNP:rs11980797).
FT /FTId=VAR_050159.
FT CONFLICT 255 255 L -> M (in Ref. 1; CAD98087).
FT CONFLICT 285 285 S -> L (in Ref. 2; BAB15667).
FT CONFLICT 706 706 K -> R (in Ref. 2; BAB15667).
SQ SEQUENCE 904 AA; 97502 MW; A2C360EDDEFFA2EF CRC64;
MAAIRALQQW CRQQCEGYRD VNICNMTTSF RDGLAFCAIL HRHRPDLINF SALKKENIYE
NNKLAFRVAE EHLGIPALLD AEDMVALKVP DRLSILTYVS QYYNYFHGRS PIGGMAGVKR
ASEDSEEEPS GKKAPVQAAK LPSPAPARKP PLSPAQTNPV VQRRNEGAGG PPPKTDQALA
GSLVSSTCGV CGKHVHLVQR HLADGRLYHR SCFRCKQCSC TLHSGAYKAT GEPGTFVCTS
HLPAAASASP KLTGLVPRQP GAMGVDSRTS CSPQKAQEAN KARPSAWEPA AGNSPARASV
PAAPNPAATS ATSVHVRSPA RPSESRLAPT PTEGKVRPRV TNSSPMGWSS AAPCTAAAAS
HPAVPPSAPD PRPATPQGGG APRVAAPQTT LSSSSTSAAT VDPPAWTPSA SRTQQARNKF
FQTSAVPPGT SLSGRGPTPS LVLSKDSSKE QARNFLKQAL SALEEAGAPA PGRPSPATAA
VPSSQPKTEA PQASPLAKPL QSSSPRVLGL PSRMEPPAPL STSSTSQASA LPPAGRRNLA
ESSGVGRVGA GSRPKPEAPM AKGKSTTLTQ DMSTSLQEGQ EDGPAGWRAN LKPVDRRSPA
ERTLKPKEPR ALAEPRAGEA PRKVSGSFAG SVHITLTPVR PDRTPRPASP GPSLPARSPS
PPRRRRLAVP ASLDVCDNWL RPEPPGQEAR VQSWKEEEKK PHLQGKPGRP LSPANVPALP
GETVTSPVRL HPDYLSPEEI QRQLQDIERR LDALELRGVE LEKRLRAAEG DDAEDSLMVD
WFWLIHEKQL LLRQESELMY KSKAQRLEEQ QLDIEGELRR LMAKPEALKS LQERRREQEL
LEQYVSTVND RSDIVDSLDE DRLREQEEDQ MLRDMIEKLG LQRKKSKFRL SKIWSPKSKS
SPSQ
//