Q967F4 (HMR1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cadherin-related hmr-1

Alternative name(s):
Protein Hammerhead

Gene names

Name:	hmr-1
ORF Names:	W02B9.1

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	2920 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Isoform A is required for cell migration during body enclosure and cell shape changes during body elongation. Required for proper localization of other junctional components, such as hmp-1, hmp-2 and jac-1. Isoform b is involved in axonal guidance in a subset of motor neurons. Ref.1 Ref.2 Ref.5
Subunit structure	Isoform a interacts with hmp-2 and jac-1. Ref.4 Ref.5
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: Isoform a is located at adherens junctions. Ref.1 Ref.5
Tissue specificity	Isoform b is neuron-specific. Isoform a is located in epidermal cells (at protein level). Ref.1 Ref.2
Developmental stage	Isoform a is present in all embryonic blastomeres at early stages of development (at protein level). Ref.1
Disruption phenotype	Morphogenetic defects before the start of body elongation, due to improper closure of hypodermis. Ref.1
Sequence similarities	Contains 14 cadherin domains. Contains 2 EGF-like domains. Contains 1 laminin G-like domain. Contains 1 TSP N-terminal (TSPN) domain.

Ontologies

Keywords
Biological process	Cell adhesion Differentiation Neurogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apical constriction involved in gastrulation Inferred from genetic interaction. Source: WormBase axonal fasciculation Inferred from mutant phenotype Ref.2. Source: WormBase body morphogenesis Inferred from mutant phenotype. Source: WormBase cell migration involved in gastrulation Inferred from genetic interaction. Source: WormBase cytoskeletal anchoring at plasma membrane Inferred from mutant phenotype Ref.1. Source: WormBase dauer entry Inferred from mutant phenotype. Source: WormBase embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase establishment of mitotic spindle orientation Inferred from mutant phenotype. Source: WormBase homophilic cell adhesion Inferred from electronic annotation. Source: InterPro receptor-mediated endocytosis Inferred from mutant phenotype. Source: WormBase reproduction Inferred from mutant phenotype. Source: WormBase
Cellular component	catenin complex Inferred from physical interaction Ref.4. Source: WormBase cell-cell adherens junction Inferred from direct assay Ref.1. Source: WormBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-catenin binding Inferred from physical interaction Ref.4Ref.5. Source: WormBase calcium ion binding Inferred from electronic annotation. Source: InterPro delta-catenin binding Inferred from physical interaction Ref.5. Source: WormBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hmp-2	O44326	5	EBI-2528888,EBI-317320

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform b (identifier: Q967F4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform a (identifier: Q967F4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1697: Missing.
     1698-1805: TYQLSEESDY...TDRDAGDTAR → MPETRQGRSS...DPSNPMYNFS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 2920	2901	Cadherin-related hmr-1		PRO_0000268646
Regions
	Topological domain	20 – 2779	2760	Extracellular Potential
	Transmembrane	2780 – 2800	21	Helical; Potential
	Topological domain	2801 – 2920	120	Cytoplasmic Potential
	Domain	322 – 422	101	Cadherin 1
	Domain	425 – 530	106	Cadherin 2
	Domain	531 – 642	112	Cadherin 3
	Domain	643 – 747	105	Cadherin 4
	Domain	749 – 865	117	Cadherin 5
	Domain	871 – 979	109	Cadherin 6
	Domain	980 – 1093	114	Cadherin 7
	Domain	1097 – 1211	115	Cadherin 8
	Domain	1212 – 1335	124	Cadherin 9
	Domain	1336 – 1436	101	Cadherin 10
	Domain	1438 – 1546	109	Cadherin 11
	Domain	1548 – 1661	114	Cadherin 12
	Domain	1662 – 1772	111	Cadherin 13
	Domain	1772 – 1874	103	Cadherin 14
	Domain	2246 – 2283	38	EGF-like 1
	Domain	2284 – 2478	195	Laminin G-like
	Domain	2312 – 2461	150	TSP N-terminal
	Domain	2492 – 2527	36	EGF-like 2
Amino acid modifications
	Glycosylation	72	1	N-linked (GlcNAc...) Potential
	Glycosylation	243	1	N-linked (GlcNAc...) Potential
	Glycosylation	253	1	N-linked (GlcNAc...) Potential
	Glycosylation	339	1	N-linked (GlcNAc...) Potential
	Glycosylation	508	1	N-linked (GlcNAc...) Potential
	Glycosylation	658	1	N-linked (GlcNAc...) Potential
	Glycosylation	685	1	N-linked (GlcNAc...) Potential
	Glycosylation	715	1	N-linked (GlcNAc...) Potential
	Glycosylation	826	1	N-linked (GlcNAc...) Potential
	Glycosylation	1177	1	N-linked (GlcNAc...) Potential
	Glycosylation	1417	1	N-linked (GlcNAc...) Potential
	Glycosylation	1646	1	N-linked (GlcNAc...) Potential
	Glycosylation	1935	1	N-linked (GlcNAc...) Potential
	Glycosylation	2224	1	N-linked (GlcNAc...) Potential
	Glycosylation	2232	1	N-linked (GlcNAc...) Potential
	Glycosylation	2307	1	N-linked (GlcNAc...) Potential
	Glycosylation	2332	1	N-linked (GlcNAc...) Potential
	Glycosylation	2623	1	N-linked (GlcNAc...) Ref.6 Ref.7
	Disulfide bond	2250 ↔ 2261		By similarity
	Disulfide bond	2255 ↔ 2270		By similarity
	Disulfide bond	2272 ↔ 2282		By similarity
	Disulfide bond	2452 ↔ 2478		By similarity
	Disulfide bond	2501 ↔ 2515		By similarity
	Disulfide bond	2517 ↔ 2526		By similarity
Natural variations
	Alternative sequence	1 – 1697	1697	Missing in isoform a.		VSP_021978
	Alternative sequence	1698 – 1805	108	TYQLS…GDTAR → MPETRQGRSSRGNCVIFGSS KRLWVTLLGFCFVLSTLIGG AEAFTDLSLPFGLEPSVAKS RFSSLVGGVRARDIHVFVMK NISEDTPVGTVLETFKAHDP SNPMYNFS in isoform a.		VSP_021979

Sequences

	Sequence		Length	Mass (Da)
	Isoform b [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 5E0D4C8FD24694FB	FASTA	2,920	323,914
	10 20 30 40 50 60 MSWNILLILL ISNLDEVLAK TLLKLPSNAP PGWLISDLQF QNLIGDSEIA TLQPSIFSTN 70 80 90 100 110 120 FEVEDGYRII TNTTVTQFHG ELFELFLNVK EQNFQRLVTL HVYVDPRGTS QQPATFLSTV 130 140 150 160 170 180 YHATVYTSQQ PGSTVVFSKP ITVRNRKNFV ISPISKIDKI SKYSSPFSVM TRGKSVDIVM 190 200 210 220 230 240 MKQKLEEDDI TRHVIFLGAF TEKTGEMIAQ TKVIIDVIDS GDVHFLLKSK KSIAKFASAI 250 260 270 280 290 300 PANSTVFDVE KRNLSEPLLF HLEEPSRFFK IDQFSGRVST VLPVGYGTYH IHVVARNQKK 310 320 330 340 350 360 QRSDAWLEIS VKKEQKLEPM TSSRSRRHLD DIVFRIPENT TMEDIEKKDM KIPLFAGETI 370 380 390 400 410 420 GEINVAKEWL KIDDDGKIHL LKPLNYEKTS SIIATVPING LQSTRTQTIR IHVADIDEPP 430 440 450 460 470 480 SFVNSPLPML AVVPLNPTIG RIVYQFVARD EHGDGDSNVL YKTIDVIPAG SFIVDPKSGV 490 500 510 520 530 540 VRTGWSKYER GDTYRISAQA MDLSPSDNTT SQLSEVAILE ILADERPPQF AKQEYEVTVS 550 560 570 580 590 600 EDNLVDYSVV DVKAQSFRSF EDGRSKGPIT YSLEGDTPED ETKWFRIDPS TGIIHLTRLL 610 620 630 640 650 660 DFDDPALPKL HKLKVTARED NRESHVDLTI RIDDVNDNVP TFTRPLYTAQ VREDIPLNQT 670 680 690 700 710 720 ILKVTAVDKD TGDNSRITYS VDNHNFSINS NGEISAKVRL DADQLNERHF VYRFNVTARD 730 740 750 760 770 780 HGEPVSLSSS AMIHIRTENT NDESAVFLPT SQYTAFVAED AQGGTPVIQI QARDADRDEV 790 800 810 820 830 840 TYSFMDKNGR STQKMNLFSI DEHTGLVKLR HGVSAADLAE AENPINLTVI VQDDGSCCVY 850 860 870 880 890 900 PSKTHTSYAT LLIGIEDVNN NKPEFPDCAK YSDIAKIMEG TYKTDPPTIV KVEATDDDSS 910 920 930 940 950 960 ANGDIVYSLY YTQSESRKAF VIDRQTGVLT PSPHVVFDRE TRPREDVTVK ATDRGDRPLI 970 980 990 1000 1010 1020 GFCQFSVEVV DINDNSPQFE RPSYETSVSR FEAVGTSVIT VFAFDNDAAH NAEITYSLEI 1030 1040 1050 1060 1070 1080 DTTAGEEHQN DLDFFELVNR RSGEITLIKP IPMKTQKFIF NVIADDNGIP EALQSSAQVT 1090 1100 1110 1120 1130 1140 LNVLDKQQKA PKWQTSPDCK PGITVDENVE LNKVILRCRA VSSGDSRNSD VIYKLTASGG 1150 1160 1170 1180 1190 1200 PGNKAESKFR QFNKFENGNE WVEVVIMEGL DYEQVNNYTL TLTATDMTSR VASTKTFVVE 1210 1220 1230 1240 1250 1260 VRDVNDVVPQ FTVDLFTGTI DEEMTPNEHL EKTNGKPIVT VKAIDTDSDG PQNEVHYRIV 1270 1280 1290 1300 1310 1320 GEANGEETKH FRIDELTGEI FPNEKFDREK IDMYILTVEA SDRSVSALPG ANGPNKDNVK 1330 1340 1350 1360 1370 1380 VQIVINDVND NAPSFEEQKY IGRVKESEGE GHDVITIKAH DLDKHSNLRY HLIGAGGGRI 1390 1400 1410 1420 1430 1440 PFGVRTDSGT IFVKEPLDFE ASDQYHLVLI ASDGRHNATT NVYIHIEDVN DNAPQFEQQK 1450 1460 1470 1480 1490 1500 YATTVIEEDV DIPKVLFNVH ATDADQDEKS SRIVYRLEGQ GADEVFRIGK YSGTIELVKA 1510 1520 1530 1540 1550 1560 LDRDPPAGVP SWNFVVQAID DDGNGLVGYA DVQVNVRDIN DNSPIFPERL FGYIEENREP 1570 1580 1590 1600 1610 1620 IHSDGVYFMD VQARDFDDPT TENANIEYGI VRNKLINGES VFRIDQNTGK IFAMRSLDRE 1630 1640 1650 1660 1670 1680 ISSEREFIIE VRANDRGVPS REGFANVTIK VTDMNDNAPF FEKTRYEGSV EETAPIGAAV 1690 1700 1710 1720 1730 1740 MSFSAFDADE EAKDNVFTYQ LSEESDYFYV TTDKDSKQSS VGVLRVKQPL DYEDVTQRDG 1750 1760 1770 1780 1790 1800 FHLGIRVSDG RHDAEAAVHV ALVDRNDHAP HIHGATEHRV REDVPRGTSI GRYTATDRDA 1810 1820 1830 1840 1850 1860 GDTARFRINR QSDPKRQFTI DQDGTLRVAH TLDREDIAVY NLIIEAYDNS NNIGRQMVAV 1870 1880 1890 1900 1910 1920 YLQDVNDNGP EPYTVPRPCI FRENTPVNQL GTCEIRATDR DTAEFGPPFT MEVSPSFKYS 1930 1940 1950 1960 1970 1980 QYLNVIFNAN GDGGNGSMTI TPLQEFDREA PVPGKILEIP LILADRAGRR NEASVHVIIG 1990 2000 2010 2020 2030 2040 DLNDNTMHDG RMTIHVNSYL GRLKETVIGR VYVDDADDWD LGDKTFSWKD SRPGFELSDK 2050 2060 2070 2080 2090 2100 GSITMAGEMA AGTYTMSANV HDNARDEDAV GYVTVIVNAV PQIAFDNQGS VQLLIAEETP 2110 2120 2130 2140 2150 2160 LQLPDDFIRA DSNGQSLMDT FKQEMTAYMG GDVTVDVFSV QVGIATLQTR DVPVLNVRFN 2170 2180 2190 2200 2210 2220 ARGSTYRDTA QLNGLIAAHR ADLQRKLNVE IVGVGIDMCK FTQCDAGCQT LNSADYDGIV 2230 2240 2250 2260 2270 2280 VSANSTVIVG VNATSRDDCT CPVWRAPPAC QHSLCHNDGV CHNTNPGFFC ECRNDGLKGA 2290 2300 2310 2320 2330 2340 RCQGTTRSFG GNGFAWYKPM PACTSLNISF SFMTTQSDAL LFYNGPLETL RNDTHIEYSD 2350 2360 2370 2380 2390 2400 YIFIQLRGGR ISLEVSMNGQ SRSSLEVAST ALNDGTWHDI SVNQEGKRVE LVVDNCRFLG 2410 2420 2430 2440 2450 2460 AGADDSSCRA ELYTPDDDER LNIVTPVQIG GLAPLSGQDY PQTIPRAGLN GCVRNLNVNG 2470 2480 2490 2500 2510 2520 DQYDLATPAF EQNSEKGCRL WGATCDSNSV DSLNHCIHGD CFADVQGSGA MVAKCVCDPG 2530 2540 2550 2560 2570 2580 WGGARCERRM EWIQFAQGAF IEYSPRIAFP EQVSDIELLF ISGKVNGAPA ELSFGTDSQQ 2590 2600 2610 2620 2630 2640 SYVSTNLESG QNGVTAAGKF DIGTGGRRAR QELRVSEVLL KENASYWLQF TRNPTRASLS 2650 2660 2670 2680 2690 2700 IDNAYTVSTQ LDKGEPFSLQ VNQITLGTQG QNKGFQGCIG TYRWSKQNLP LKRGGAMDEN 2710 2720 2730 2740 2750 2760 EESIVSISNM AGVQDGCDLR ITCADLPAGY CGGSFVCVDF WKGPFCTCND GANAILGDDG 2770 2780 2790 2800 2810 2820 QVVGCGETLA VSKLGISSPA IILILVSLAL LILLVMMMVV YTRRSPGAFE NVRPEEMNRD 2830 2840 2850 2860 2870 2880 NLRQYGVEGG GEADNDQYSM AGLRKPVMPL DTGMGPAIGG HPPHYPPRGM APPKDDHELN 2890 2900 2910 2920 SKIKDLETDQ NAAPYDELRI YDDERDNISV VTLESIESAQ
	Isoform a [UniParc]. Checksum: 095CD0C74F4AAB82	FASTA	1,223	133,483
	10 20 30 40 50 60 MPETRQGRSS RGNCVIFGSS KRLWVTLLGF CFVLSTLIGG AEAFTDLSLP FGLEPSVAKS 70 80 90 100 110 120 RFSSLVGGVR ARDIHVFVMK NISEDTPVGT VLETFKAHDP SNPMYNFSFR INRQSDPKRQ 130 140 150 160 170 180 FTIDQDGTLR VAHTLDREDI AVYNLIIEAY DNSNNIGRQM VAVYLQDVND NGPEPYTVPR 190 200 210 220 230 240 PCIFRENTPV NQLGTCEIRA TDRDTAEFGP PFTMEVSPSF KYSQYLNVIF NANGDGGNGS 250 260 270 280 290 300 MTITPLQEFD REAPVPGKIL EIPLILADRA GRRNEASVHV IIGDLNDNTM HDGRMTIHVN 310 320 330 340 350 360 SYLGRLKETV IGRVYVDDAD DWDLGDKTFS WKDSRPGFEL SDKGSITMAG EMAAGTYTMS 370 380 390 400 410 420 ANVHDNARDE DAVGYVTVIV NAVPQIAFDN QGSVQLLIAE ETPLQLPDDF IRADSNGQSL 430 440 450 460 470 480 MDTFKQEMTA YMGGDVTVDV FSVQVGIATL QTRDVPVLNV RFNARGSTYR DTAQLNGLIA 490 500 510 520 530 540 AHRADLQRKL NVEIVGVGID MCKFTQCDAG CQTLNSADYD GIVVSANSTV IVGVNATSRD 550 560 570 580 590 600 DCTCPVWRAP PACQHSLCHN DGVCHNTNPG FFCECRNDGL KGARCQGTTR SFGGNGFAWY 610 620 630 640 650 660 KPMPACTSLN ISFSFMTTQS DALLFYNGPL ETLRNDTHIE YSDYIFIQLR GGRISLEVSM 670 680 690 700 710 720 NGQSRSSLEV ASTALNDGTW HDISVNQEGK RVELVVDNCR FLGAGADDSS CRAELYTPDD 730 740 750 760 770 780 DERLNIVTPV QIGGLAPLSG QDYPQTIPRA GLNGCVRNLN VNGDQYDLAT PAFEQNSEKG 790 800 810 820 830 840 CRLWGATCDS NSVDSLNHCI HGDCFADVQG SGAMVAKCVC DPGWGGARCE RRMEWIQFAQ 850 860 870 880 890 900 GAFIEYSPRI AFPEQVSDIE LLFISGKVNG APAELSFGTD SQQSYVSTNL ESGQNGVTAA 910 920 930 940 950 960 GKFDIGTGGR RARQELRVSE VLLKENASYW LQFTRNPTRA SLSIDNAYTV STQLDKGEPF 970 980 990 1000 1010 1020 SLQVNQITLG TQGQNKGFQG CIGTYRWSKQ NLPLKRGGAM DENEESIVSI SNMAGVQDGC 1030 1040 1050 1060 1070 1080 DLRITCADLP AGYCGGSFVC VDFWKGPFCT CNDGANAILG DDGQVVGCGE TLAVSKLGIS 1090 1100 1110 1120 1130 1140 SPAIILILVS LALLILLVMM MVVYTRRSPG AFENVRPEEM NRDNLRQYGV EGGGEADNDQ 1150 1160 1170 1180 1190 1200 YSMAGLRKPV MPLDTGMGPA IGGHPPHYPP RGMAPPKDDH ELNSKIKDLE TDQNAAPYDE 1210 1220 LRIYDDERDN ISVVTLESIE SAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo." Costa M., Raich W., Agbunag C., Leung B., Hardin J., Priess J.R. J. Cell Biol. 141:297-308(1998) [PubMed: 9531567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: Bristol N2.
[2]	"The C. elegans hmr-1 gene can encode a neuronal classic cadherin involved in the regulation of axon fasciculation." Broadbent I.D., Pettitt J. Curr. Biol. 12:59-63(2002) [PubMed: 11790304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, FUNCTION. Strain: Bristol N2.
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[4]	"Distinct beta-catenins mediate adhesion and signalling functions in C. elegans." Korswagen H.C., Herman M.A., Clevers H.C. Nature 406:527-532(2000) [PubMed: 10952315] [Abstract] Cited for: INTERACTION WITH HMP-2.
[5]	"The Caenorhabditis elegans p120 catenin homologue, JAC-1, modulates cadherin-catenin function during epidermal morphogenesis." Pettitt J., Cox E.A., Broadbent I.D., Flett A., Hardin J. J. Cell Biol. 162:15-22(2003) [PubMed: 12847081] [Abstract] Cited for: INTERACTION WITH JAC-1, SUBCELLULAR LOCATION, FUNCTION.
[6]	"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2623, MASS SPECTROMETRY. Strain: Bristol N2.
[7]	"Identification of the hydrophobic glycoproteins of Caenorhabditis elegans." Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J. Glycobiology 15:952-964(2005) [PubMed: 15888633] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2623, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF016854 mRNA. Translation: AAB94553.1. AJ307058 mRNA. Translation: CAC38842.1. Z82064 Genomic DNA. Translation: CAB61036.1. Z82064, AL032638, Z82093 Genomic DNA. Translation: CAD27611.1. AL032638, Z82064, Z82093 Genomic DNA. Translation: CAD27619.1. Z82093, AL032638, Z82064 Genomic DNA. Translation: CAD27620.1.
RefSeq	NP_001021649.1. NM_001026478.2. NP_001021650.1. NM_001026479.1.
UniGene	Cel.17110.
3D structure databases
HSSP	HSSP built from PDB template 2A4C based on UniProtKB P55288.
ProteinModelPortal	Q967F4.
SMR	Q967F4. Positions 368-2080, 2245-2466, 2495-2532, 2718-2755, 2866-2920.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q967F4. 2 interactions.
STRING	Q967F4.
Proteomic databases
PRIDE	Q967F4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	W02B9.1b.1; W02B9.1b.1; W02B9.1. W02B9.1b.2; W02B9.1b.2; W02B9.1.
GeneID	173007.
KEGG	cel:W02B9.1.
UCSC	W02B9.1b. c. elegans.
Organism-specific databases
CTD	173007.
WormBase	W02B9.1a; CE25133; WBGene00001980; hmr-1. W02B9.1b; CE30357; WBGene00001980; hmr-1.
Phylogenomic databases
eggNOG	meNOG05349.
GeneTree	EMGT00050000004967.
InParanoid	Q967F4.
OMA	NGEVKYG.
PhylomeDB	Q967F4.
Gene expression databases
ArrayExpress	Q967F4.
Family and domain databases
InterPro	IPR002126. Cadherin. IPR015919. Cadherin-like. IPR020894. Cadherin_CS. IPR000233. Cadherin_cytoplasmic-dom. IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. IPR018247. EF_Hand_1_Ca_BS. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR000742. EGF_3. IPR001791. Laminin_G. IPR012680. Laminin_G_2. [Graphical view]
Gene3D	G3DSA:2.60.40.60. Cadherin. 14 hits. G3DSA:2.60.120.200. ConA_like_subgrp. 2 hits.
Pfam	PF00028. Cadherin. 8 hits. PF01049. Cadherin_C. 1 hit. PF02210. Laminin_G_2. 1 hit. [Graphical view]
PRINTS	PR00205. CADHERIN.
SMART	SM00112. CA. 13 hits. SM00181. EGF. 2 hits. SM00282. LamG. 1 hit. [Graphical view]
SUPFAM	SSF49313. Cadherin. 15 hits. SSF49899. ConA_like_lec_gl. 2 hits.
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS00232. CADHERIN_1. 8 hits. PS50268. CADHERIN_2. 15 hits. PS00018. EF_HAND_1. 1 hit. PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 2 hits. PS50025. LAM_G_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	877893.

Entry information

Entry name

HMR1_CAEEL

Accession

Primary (citable) accession number: Q967F4
Secondary accession number(s): O44327

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project